KEGG   ENZYME: 2.7.11.32
Entry
EC 2.7.11.32                Enzyme                                 
Name
[pyruvate, phosphate dikinase] kinase;
PPDK regulatory protein (ambiguous);
pyruvate;
phosphate dikinase regulatory protein (ambiguous);
bifunctional dikinase regulatory protein (ambiguous)
Class
Transferases;
Transferring phosphorus-containing groups;
Protein-serine/threonine kinases
Sysname
ADP:[pyruvate, phosphate dikinase] phosphotransferase
Reaction(IUBMB)
ADP + [pyruvate, phosphate dikinase] = AMP + [pyruvate, phosphate dikinase] phosphate
Substrate
ADP [CPD:C00008];
[pyruvate, phosphate dikinase]
Product
AMP [CPD:C00020];
[pyruvate, phosphate dikinase] phosphate
Comment
The enzymes from the plants Zea mays (maize) and Arabidopsis thaliana are bifunctional and catalyse both the phosphorylation and dephosphorylation of EC 2.7.9.1 (pyruvate, phosphate dikinase). cf. EC 2.7.4.27, [pyruvate, phosphate dikinase]-phosphate phosphotransferase [2-5]. The enzyme is specific for a reaction intermediate form of EC 2.7.9.1, and phosphorylates a threonine located adjacent to the catalytic histidine. The phosphorylation only takes place if the histidine is already phosphorylated [3-5].
History
EC 2.7.11.32 created 2012
Orthology
K20115  [pyruvate, phosphate dikinase]-phosphate phosphotransferase / [pyruvate, phosphate dikinase] kinase
Genes
ATHAT3G01200(RP2) AT4G21210(RP1)
ALY9303932 9320356
CRB17878882 17892435
CSAT104698933 104718210 104722939 104731423 104744240 104763839
EUSEUTSA_v10020923mg EUTSA_v10025354mg
BRP103842753 103858872 103870958
BNA106345705 106404071 106406424 106435635 106438335 106440302
BOE106293872 106296714 106341208 106342598
RSZ108805601 108843126 108857170
THJ104812524 104821035
CPAP110806752 110806754
CIT102625399
CICCICLE_v10015558mg
PVY116109174
MINC123193251
TCC18597088
GRA105773645
GHI107901928 107961963
GAB108485543
DZI111318795
EGR104441127
GMX100137073 100794046
GSJ114369815 114403013
PVUPHAVU_007G051900g
VRA106754378 106770993
VAR108326098
VUN114191113
CCAJ109794396
APRC113871554
MTR25485252
CAM101507702
LJALj5g3v2060750.1(Lj5g3v2060750.1)
ADU107467154
AIP107617832
AHF112711854 112775371
LANG109336124
FVE101308056
RCN112167739
PPER18780113
PMUM103324490
PAVI110763034
PDUL117624713
MDM103434542
PXB103933007 103941131 103948128 103955392
ZJU107421062
MNT21397940
CSV101220007
CMO103485569
BHJ120083768
MCHA111010787
CMAX111495454
CMOS111440043
CPEP111782979
RCU8267381
JCU105649393
HBR110636619
MESC110603622
POP7458550
PEU105113246
PALZ118059559
JRE108983234
QSU112031681
QLO115989663 115990842
TWL120004904
VVI100267490
VRI117923608
SLY101255037
SPEN107002608
SOT102594017
SSTN125865181
CANN107845493
NTA107773333 107815559
NSY104225429
NTO104109587
NAU109230999
INI109165297
ITR116032394
SIND105167965
OEU111396000
EGT105962251
SSPL121802963 121807033
HAN110939674 110943399
ECAD122582002 122591136
LSV111907253 111908122
CCAV112522825
DCR108209066
CSIN114310070 114310078
BVG104901122
SOE110799056
CQI110731396
NNU104585674 104604896
MING122092124
TSS122640309
PSOM113287860 113304396
NCOL116251543
OSA4343450
DOSAOs07t0530600-01(Os07g0530600)
OBR102710420
BDI100839068
ATS109748005
TDC119354275 119363439
TAES123044640 123052525 123188396
TUA125536806
SBI110432938 8080149 8084066
ZMA100279565 732785
SITA101777229
SVS117843718
PVIR120661558 120690138
PHAI112879833
PDA103715354 103715355
EGU105052107 105052116
MUS103986573
DCT110106594
PEQ110022763
AOF109833321
ATR18440240
SMOSELMODRAFT_120503 SELMODRAFT_33587
PPP112288144
CRECHLRE_12g514600v5
VCNVOLCADRAFT_43639
OLUOSTLU_33216
OTAOT_ostta08g03490
MISMICPUN_60800
MPPMICPUCDRAFT_58264
SMINv1.2.014430.t1(symbB.v1.2.014430.t1) v1.2.022569.t1(symbB.v1.2.022569.t1) v1.2.027162.t1(symbB.v1.2.027162.t1) v1.2.040824.t3(symbB.v1.2.040824.t3)
PTIPHATRDRAFT_49027
FCYFRACYDRAFT_291525
GTTGUITHDRAFT_43527 GUITHDRAFT_43962 GUITHDRAFT_85988
SCLsce5851
SCUSCE1572_34845
CCROCMC5_073520
SAMYDB32_004705
LLUAKJ09_03979
MRMA7982_11854
 » show all
Reference
1  [PMID:6326674]
  Authors
Burnell JN, Hatch MD
  Title
Regulation of C4 photosynthesis: identification of a catalytically important histidine residue and its role in the regulation of pyruvate,Pi dikinase.
  Journal
Arch Biochem Biophys 231:175-82 (1984)
DOI:10.1016/0003-9861(84)90375-8
  Sequence
[zma:732785]
Reference
2  [PMID:2983615]
  Authors
Burnell JN, Hatch MD
  Title
Regulation of C4 photosynthesis: purification and properties of the protein catalyzing ADP-mediated inactivation and Pi-mediated activation of pyruvate,Pi dikinase.
  Journal
Arch Biochem Biophys 237:490-503 (1985)
DOI:10.1016/0003-9861(85)90302-9
  Sequence
[zma:732785]
Reference
3  [PMID:10683263]
  Authors
Chastain CJ, Botschner M, Harrington GE, Thompson BJ, Mills SE, Sarath G, Chollet R
  Title
Further analysis of maize C(4) pyruvate,orthophosphate dikinase phosphorylation by its bifunctional regulatory protein using selective substitutions of the regulatory Thr-456 and catalytic His-458 residues.
  Journal
Arch Biochem Biophys 375:165-70 (2000)
DOI:10.1006/abbi.1999.1651
  Sequence
[zma:732785]
Reference
4  [PMID:16696949]
  Authors
Burnell JN, Chastain CJ
  Title
Cloning and expression of maize-leaf pyruvate, Pi dikinase regulatory protein gene.
  Journal
Biochem Biophys Res Commun 345:675-80 (2006)
DOI:10.1016/j.bbrc.2006.04.150
  Sequence
[zma:732785]
Reference
5  [PMID:17996018]
  Authors
Chastain CJ, Xu W, Parsley K, Sarath G, Hibberd JM, Chollet R
  Title
The pyruvate, orthophosphate dikinase regulatory proteins of Arabidopsis possess a novel, unprecedented Ser/Thr protein kinase primary structure.
  Journal
Plant J 53:854-63 (2008)
DOI:10.1111/j.1365-313X.2007.03366.x
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 2.7.11.32
IUBMB Enzyme Nomenclature: 2.7.11.32
ExPASy - ENZYME nomenclature database: 2.7.11.32
BRENDA, the Enzyme Database: 2.7.11.32

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