DB code: D00127
CATH domain | 1.10.135.10 : Transferase Creatine Kinase; Chain A, domain 1 | |
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3.30.590.10 : Creatine Kinase; Chain A, domain 2 | Catalytic domain | |
E.C. | 2.7.3.3 | |
CSA | 1bg0 | |
M-CSA | 1bg0 | |
MACiE | M0086 |
CATH domain | Related DB codes (homologues) |
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Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | Pfam |
---|---|---|---|
P51541 |
Arginine kinase
|
AK
EC 2.7.3.3 |
PF00217
(ATP-gua_Ptrans)
PF02807 (ATP-gua_PtransN) [Graphical View] |
KEGG enzyme name |
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arginine kinase
arginine phosphokinase adenosine 5'-triphosphate: L-arginine phosphotransferase adenosine 5'-triphosphate-arginine phosphotransferase ATP:L-arginine N-phosphotransferasel ATP:L-arginineomega-N-phosphotransferase |
UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
---|---|---|---|---|---|
P51541 | KARG_LIMPO | ATP + L-arginine = ADP + N(omega)-phospho-L- arginine. | Monomer. | Cytoplasm. |
KEGG Pathways | Map code | Pathways | E.C. |
---|---|---|
MAP00330 | Arginine and proline metabolism |
Compound table | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|
Cofactors | Substrates | Products | Intermediates | ||||||||
KEGG-id | C00305 | C00002 | C00062 | C00008 | C05945 | ||||||
E.C. | |||||||||||
Compound | Magnesium | ATP | L-Arginine | ADP | N-Phospho-L-arginine | ||||||
Type | divalent metal (Ca2+, Mg2+) | amine group,nucleotide | amino acids,amine group,imine group,lipid | amine group,nucleotide | amino acids,amine group,imine group,lipid,phosphate group/phosphate ion | ||||||
ChEBI |
18420 18420 |
15422 15422 |
16467 16467 |
16761 16761 |
18412 18412 |
||||||
PubChem |
888 888 |
5957 5957 |
28782 6322 28782 6322 |
6022 6022 |
92150 92150 |
||||||
1bg0A01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||||
1m80A01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||||
1m80B01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||||
1m15A01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||||
1p50A01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||||
1p52A01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||||
1bg0A02 | Bound:_MG | Unbound | Analogue:DAR | Bound:ADP | Unbound | Transition-state-analogue:NO3_401 | |||||
1m80A02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||||
1m80B02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||||
1m15A02 | Bound:_MG | Unbound | Bound:ARG | Bound:ADP | Unbound | Transition-state-analogue:NO3_405 | |||||
1p50A02 | Bound:_MG | Unbound | Bound:ARG | Bound:ADP | Unbound | Transition-state-analogue:NO3 | |||||
1p52A02 | Bound:_MG | Unbound | Analogue:DAR | Bound:ADP | Unbound | Transition-state-analogue:NO3_401 |
Reference for Active-site residues | ||
---|---|---|
resource | references | E.C. |
Swiss-prot;P51541 |
Active-site residues | ||||||||||
---|---|---|---|---|---|---|---|---|---|---|
PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
1bg0A01 | ||||||||||
1m80A01 | ||||||||||
1m80B01 | ||||||||||
1m15A01 | ||||||||||
1p50A01 | ||||||||||
1p52A01 | ||||||||||
1bg0A02 | CYS 271 | |||||||||
1m80A02 | CYS 271 | |||||||||
1m80B02 | CYS 271 | |||||||||
1m15A02 | CYS 271 | |||||||||
1p50A02 | CYS 271 | |||||||||
1p52A02 | CYS 271 |
References for Catalytic Mechanism | ||
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References | Sections | No. of steps in catalysis |
[4]
|
Fig.3, p.8451-8453 | |
[10]
|
p.26956-26957 |
References | |
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[1] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 7819288 |
Journal | Biochim Biophys Acta |
Year | 1995 |
Volume | 1246 |
Pages | 197-200 |
Authors | Strong SJ, Ellington WR |
Title |
Isolation and sequence analysis of the gene for arginine kinase from the chelicerate arthropod, |
Related PDB | |
Related UniProtKB | |
[2] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 9359868 |
Journal | Biochem J |
Year | 1997 |
Volume | 328 |
Pages | 301-6 |
Authors | Suzuki T, Kawasaki Y, Furukohri T |
Title |
Evolution of phosphagen kinase. |
Related PDB | |
Related UniProtKB | |
[3] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 9675202 |
Journal | Biophys J |
Year | 1998 |
Volume | 75 |
Pages | 1016-23 |
Authors | Forstner M, Kriechbaum M, Laggner P, Wallimann T |
Title | Structural changes of creatine kinase upon substrate binding. |
Related PDB | |
Related UniProtKB | |
[4] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) |
Medline ID | 98337935 |
PubMed ID | 9671698 |
Journal | Proc Natl Acad Sci U S A |
Year | 1998 |
Volume | 95 |
Pages | 8449-54 |
Authors | Zhou G, Somasundaram T, Blanc E, Parthasarathy G, Ellington WR, Chapman MS |
Title | Transition state structure of arginine kinase: implications for catalysis of bimolecular reactions. |
Related PDB | 1bg0 |
Related UniProtKB | P51541 |
[5] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 10089314 |
Journal | Acta Crystallogr D Biol Crystallogr |
Year | 1999 |
Volume | 55 |
Pages | 835-45 |
Authors | Zhou G, Somasundaram T, Blanc E, Chen Z, Chapman MS |
Title | Critical initial real-space refinement in the structure determination of arginine kinase. |
Related PDB | |
Related UniProtKB | |
[6] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 10461938 |
Journal | J Parasitol |
Year | 1999 |
Volume | 85 |
Pages | 603-7 |
Authors | Platzer EG, Wang W, Thompson SN, Borchardt DB |
Title |
Arginine kinase and phosphoarginine, |
Related PDB | |
Related UniProtKB | |
[7] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 10811656 |
Journal | J Biol Chem |
Year | 2000 |
Volume | 275 |
Pages | 23884-90 |
Authors | Suzuki T, Fukuta H, Nagato H, Umekawa M |
Title |
Arginine kinase from Nautilus pompilius, |
Related PDB | |
Related UniProtKB | |
[8] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 12454458 |
Journal | Acta Crystallogr D Biol Crystallogr |
Year | 2002 |
Volume | 58 |
Pages | 2009-17 |
Authors | Yousef MS, Fabiola F, Gattis JL, Somasundaram T, Chapman MS |
Title | Refinement of the arginine kinase transition-state analogue complex at 1.2 A resolution: mechanistic insights. |
Related PDB | 1m15 |
Related UniProtKB | |
[9] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 12493833 |
Journal | Protein Sci |
Year | 2003 |
Volume | 12 |
Pages | 103-11 |
Authors | Yousef MS, Clark SA, Pruett PK, Somasundaram T, Ellington WR, Chapman MS |
Title | Induced fit in guanidino kinases--comparison of substrate-free and transition state analog structures of arginine kinase. |
Related PDB | 1m80 |
Related UniProtKB | |
[10] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 12732621 |
Journal | J Biol Chem |
Year | 2003 |
Volume | 278 |
Pages | 26952-7 |
Authors | Pruett PS, Azzi A, Clark SA, Yousef MS, Gattis JL, Somasundaram T, Ellington WR, Chapman MS |
Title |
The putative catalytic bases have, |
Related PDB | 1p50 1p52 |
Related UniProtKB |
Comments |
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Created | Updated |
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2004-03-18 | 2009-02-26 |