Q8P4D0

PR
Gene name
aceK
Protein name
Isocitrate dehydrogenase kinase/phosphatase
Names
IDH kinase/phosphatase, IDHK/P
Species
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
KEGG Pathway
xcc:XCC3780
EC number
2.7.11.5: Protein-serine/threonine kinases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-40 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q8P4D0

Entry ID Method Resolution Chain Position Source
AF-Q8P4D0-F1 Predicted AlphaFoldDB

No variants for Q8P4D0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8P4D0

No associated diseases with Q8P4D0

2 regional properties for Q8P4D0

Type Name Position InterPro Accession
domain Isocitrate dehydrogenase kinase/phosphatase (AceK), regulatory domain 19 - 314 IPR046854
domain Isocitrate dehydrogenase kinase/phosphatase (AceK), kinase domain 319 - 573 IPR046855

Functions

Description
EC Number 2.7.11.5 Protein-serine/threonine kinases
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

5 GO annotations of molecular function

Name Definition
[isocitrate dehydrogenase (NADP+)] kinase activity Catalysis of the reaction: ATP + (isocitrate dehydrogenase (NADP)) = ADP + (isocitrate dehydrogenase (NADP)) phosphate.
AMP binding Binding to AMP, adenosine monophosphate.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
phosphoprotein phosphatase activity Catalysis of the reaction: a phosphoprotein + H2O = a protein + phosphate. Together with protein kinases, these enzymes control the state of phosphorylation of cellular proteins and thereby provide an important mechanism for regulating cellular activity.
protein serine/threonine kinase activity Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate.

6 GO annotations of biological process

Name Definition
glucose metabolic process The chemical reactions and pathways involving glucose, the aldohexose gluco-hexose. D-glucose is dextrorotatory and is sometimes known as dextrose; it is an important source of energy for living organisms and is found free as well as combined in homo- and hetero-oligosaccharides and polysaccharides.
glyoxylate cycle A modification of the TCA cycle occurring in some plants and microorganisms, in which isocitrate is cleaved to glyoxylate and succinate. Glyoxylate can then react with acetyl-CoA to form malate.
peptidyl-serine phosphorylation The phosphorylation of peptidyl-serine to form peptidyl-O-phospho-L-serine.
protein dephosphorylation The process of removing one or more phosphoric residues from a protein.
regulation of catalytic activity Any process that modulates the activity of an enzyme.
tricarboxylic acid cycle A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MNQQPLPPQS ERRALAIGRA VYEAFQDYHA QFSQITARAR QRFETRDWSG AREDAVARIA
70 80 90 100 110 120
LYDHYISECM LRLRAVLLGQ AHDRALWMRA RTHYAELLTG LIDQELYKTF YNTLTRRYFR
130 140 150 160 170 180
TQGVDAQIEF IALDIEPTDA ITVPVARHTY AVSPGRLTEM LVRVLGDYPF EVPYAHRTRC
190 200 210 220 230 240
AAAIAVRLLD DLAHWGEHPV RSVELLETVF YRERRAYLVG RLFGEHRFSP CVIALVNDDA
250 260 270 280 290 300
GLRAEAVLTR RSDVAQLFSN SRSYFQADLT TVGDAVVFLR SLLTHKPIDE LYTMLGRAKQ
310 320 330 340 350 360
GKTERYRTFF RHFQAHPAEQ LVHADGTPGM VMVVFTLPSY PLVFKLIRDR FAYPKTMSRA
370 380 390 400 410 420
QVEGKYELVF QLDRIGRLLD AQPYRFLRFP KARFSPALLQ DLQSSCAMSL SEDGDDVLIA
430 440 450 460 470 480
LCYVQRRLRP LNLYLREQLP AAAHAAALDY GQAIKDMARN NIFPGDMLLK NFGITRHQRA
490 500 510 520 530 540
VFYDYDELCL ITECTFRDWP TPTSYEEQMA AEPWFHVGPR DVFPERFALF MGLPSSQLEA
550 560 570
VKHMHPELFD PQWWRDLQAR LREDDYPDTP PYADAQKLA