KEGG   ORTHOLOGY: K00934
Entry
K00934                      KO                                     

Name
E2.7.3.3
Definition
arginine kinase [EC:2.7.3.3]
Pathway
ko00330  Arginine and proline metabolism
Brite
KEGG Orthology (KO) [BR:ko00001]
 09100 Metabolism
  09105 Amino acid metabolism
   00330 Arginine and proline metabolism
    K00934  E2.7.3.3; arginine kinase
Enzymes [BR:ko01000]
 2. Transferases
  2.7  Transferring phosphorus-containing groups
   2.7.3  Phosphotransferases with a nitrogenous group as acceptor
    2.7.3.3  arginine kinase
     K00934  E2.7.3.3; arginine kinase
Other DBs
RN: R00554
GO: 0004054
Genes
TNG: GSTEN00023314G001
DME: Dmel_CG32031(Argk) Dmel_CG4546(CG4546) Dmel_CG5144(CG5144)
DER: 113563687 6545035 6552971
DSE: 6604978 6604979 6606199
DSI: Dsimw501_GD14150(Dsim_GD14150) Dsimw501_GD19054(Dsim_GD19054) Dsimw501_GD29168(Dsim_GD29168)
DYA: Dyak_GE20801 Dyak_GE21263 Dyak_GE24345
DAN: 6501321 6506151
DSR: 110190437 110190439 110191864
DPO: Dpse_GA16624 Dpse_GA18246 Dpse_GA18688
DPE: 6592100 6603018 6603019
DVI: 6631071
AAG: 5571596
AME: 550932(Argk)
MPHA: 105834340
AEC: 105152512
ACEP: 105620866
VEM: 105567573
HST: 105188133
DQU: 106740621
CFO: 105255845
LHU: 105667738
PGC: 109854282
PCF: 106792158
NVI: 100114388
MDL: 103569307
BMOR: 692924(AK)
BMAN: 114247438
PMAC: 106714164
PRAP: 111001874
HAW: 110372888
TNL: 113501645
PXY: 105390215
API: 100166732
DNX: 107163940
AGS: 114121042
RMD: 113556930
BTAB: 109033664
ZNE: 110828625
TUT: 107364130
CEL: CELE_F32B5.1(F32B5.1) CELE_F44G3.2(argk-1) CELE_F46H5.3(F46H5.3) CELE_W10C8.5(W10C8.5)
CBR: CBG04232
TSP: Tsp_06232
PCAN: 112566920
SHX: MS3_05631
AMIL: 114962238
PDAM: 113666305
HMG: 105845327
SUN: SUN_1812
PAMO: BAR1_03620
 » show all
Reference
  Authors
Pereira CA, Alonso GD, Paveto MC, Iribarren A, Cabanas ML, Torres HN, Flawia MM
  Title
Trypanosoma cruzi arginine kinase characterization and cloning. A novel energetic pathway in protozoan parasites.
  Journal
J Biol Chem 275:1495-501 (2000)
DOI:10.1074/jbc.275.2.1495
  Sequence
[tcr:507241.30]

KEGG   ENZYME: 2.7.3.3
Entry
EC 2.7.3.3                  Enzyme                                 

Name
arginine kinase;
arginine phosphokinase;
adenosine 5'-triphosphate: L-arginine phosphotransferase;
adenosine 5'-triphosphate-arginine phosphotransferase;
ATP:L-arginine N-phosphotransferasel ATP:L-arginine omega-N-phosphotransferase
Class
Transferases;
Transferring phosphorus-containing groups;
Phosphotransferases with a nitrogenous group as acceptor
Sysname
ATP:L-arginine Nomega-phosphotransferase
Reaction(IUBMB)
ATP + L-arginine = ADP + Nomega-phospho-L-arginine [RN:R00554]
Reaction(KEGG)
R00554
Substrate
ATP [CPD:C00002];
L-arginine [CPD:C00062]
Product
ADP [CPD:C00008];
Nomega-phospho-L-arginine
History
EC 2.7.3.3 created 1961
Pathway
ec00330  Arginine and proline metabolism
Orthology
K00934  arginine kinase
Genes
TNG: GSTEN00023314G001
DME: Dmel_CG32031(Argk) Dmel_CG4546(CG4546) Dmel_CG5144(CG5144)
DER: 113563687 6545035 6552971
DSE: 6604978 6604979 6606199
DSI: Dsimw501_GD14150(Dsim_GD14150) Dsimw501_GD19054(Dsim_GD19054) Dsimw501_GD29168(Dsim_GD29168)
DYA: Dyak_GE20801 Dyak_GE21263 Dyak_GE24345
DAN: 6501321 6506151
DSR: 110190437 110190439 110191864
DPO: Dpse_GA16624 Dpse_GA18246 Dpse_GA18688
DPE: 6592100 6603018 6603019
DVI: 6631071
AAG: 5571596
AME: 550932(Argk)
MPHA: 105834340
AEC: 105152512
ACEP: 105620866
VEM: 105567573
HST: 105188133
DQU: 106740621
CFO: 105255845
LHU: 105667738
PGC: 109854282
PCF: 106792158
NVI: 100114388
MDL: 103569307
BMOR: 692924(AK)
BMAN: 114247438
PMAC: 106714164
PRAP: 111001874
HAW: 110372888
TNL: 113501645
PXY: 105390215
API: 100166732
DNX: 107163940
AGS: 114121042
RMD: 113556930
BTAB: 109033664
ZNE: 110828625
TUT: 107364130
CEL: CELE_F32B5.1(F32B5.1) CELE_F44G3.2(argk-1) CELE_F46H5.3(F46H5.3) CELE_W10C8.5(W10C8.5)
CBR: CBG04232
TSP: Tsp_06232
PCAN: 112566920
SHX: MS3_05631
AMIL: 114962238
PDAM: 113666305
HMG: 105845327
SUN: SUN_1812
PAMO: BAR1_03620
 » show all
Reference
1  [PMID:13339436]
  Authors
ELODI P, SZORENYI E.
  Title
Properties of crystalline arginine-phosphoferase isolated from Crustacean muscle.
  Journal
Acta Physiol Hung 9:367-79 (1956)
Reference
2  [PMID:13403885]
  Authors
MORRISON JF, GRIFFITHS DE, ENNOR AH.
  Title
The purification and properties of arginine phosphokinase.
  Journal
Biochem J 65:143-53 (1957)
DOI:10.1042/bj0650143
Reference
3
  Authors
Szorenyi, E.T., Dvornikova, P.D. and Degtyar, P.G.
  Title
[Isolation in the crystalline state and some properties of adenosinetriphosphate-arginine transphosphorylase.].
  Journal
Dokl Akad Nauk SSSR 67:341-344 (1949)
Reference
4  [PMID:14340045]
  Authors
VIRDEN R, WATTS DC, BALDWIN E.
  Title
ADENOSINE 5'-TRIPHOSPHATE-ARGININE PHOSPHOTRANSFERASE FROM LOBSTER MUSCLE: PURIFICATION AND PROPERTIES.
  Journal
Biochem J 94:536-44 (1965)
DOI:10.1042/bj0940536
Other DBs
ExplorEnz - The Enzyme Database: 2.7.3.3
IUBMB Enzyme Nomenclature: 2.7.3.3
ExPASy - ENZYME nomenclature database: 2.7.3.3
BRENDA, the Enzyme Database: 2.7.3.3
CAS: 9026-70-4

KEGG   REACTION: R00554
Entry
R00554                      Reaction                               

Name
ATP:L-arginine Nomega-phosphotransferase
Definition
ATP + L-Arginine <=> ADP + L-Arginine phosphate
Equation
Reaction class
RC00002  C00002_C00008
RC00203  C00062_C05945
Enzyme
Pathway
rn00330  Arginine and proline metabolism
Orthology
K00934  arginine kinase [EC:2.7.3.3]
Other DBs
RHEA: 22943

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