Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

2 structures for P19824

Entry ID Method Resolution Chain Position Source
6H7G X-ray 260 A A/B 32-375 PDB
AF-P19824-F1 Predicted AlphaFoldDB

1 variants for P19824

Variant ID(s) Position Change Description Diseaes Association Provenance
95 R>C mutant 12-2B; increase in substrate affinity [UniProt] No

No associated diseases with P19824

1 regional properties for P19824

Type Name Position InterPro Accession
domain Phosphoribulokinase/uridine kinase 38 - 236 IPR006083

Functions

Description
EC Number 2.7.1.19 Phosphotransferases with an alcohol group as acceptor
Subcellular Localization
  • Plastid, chloroplast
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
chloroplast A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma.
stromule Thin filamentous structure extending from the surface of all plastid types examined so far, including chloroplast, proplastid, etioplast, leucoplast, amyloplast, and chromoplast. In general, stromules are more abundant in tissues containing non-green plastids, and in cells containing smaller plastids. The primary function of stromules is still unresolved, although the presence of stromules markedly increases the plastid surface area, potentially increasing transport to and from the cytosol. Other functions of stromules, such as transfer of macromolecules between plastids and starch granule formation in cereal endosperm, may be restricted to particular tissues and cell types.
supramolecular complex A cellular component that consists of an indeterminate number of proteins or macromolecular complexes, organized into a regular, higher-order structure such as a polymer, sheet, network or a fiber.

5 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
disordered domain specific binding Binding to a disordered domain of a protein.
enzyme binding Binding to an enzyme, a protein with catalytic activity.
phosphoribulokinase activity Catalysis of the reaction: D-ribulose 5-phosphate + ATP = D-ribulose 1,5-bisphosphate + ADP + 2 H(+).
protein homodimerization activity Binding to an identical protein to form a homodimer.

3 GO annotations of biological process

Name Definition
phosphorylation The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide.
reductive pentose-phosphate cycle The fixation of carbon dioxide (CO2) as glucose in the chloroplasts of C3 plants; uses ATP and NADPH formed in the light reactions of photosynthesis; carbon dioxide reacts with ribulose 1,5-bisphosphate (catalyzed by the function of ribulose-bisphosphate carboxylase) to yield two molecules of 3-phosphoglycerate; these are then phosphorylated by ATP to 1,3-bisphosphateglyceraldehyde which, in turn, is then reduced by NADPH to glyceraldehyde 3-phosphate. The glyceraldehyde 3-phosphate is converted to fructose 5-phosphate and ribulose 5-phosphate by aldolase and other enzymes; the ribulose 5-phosphate is phosphorylated by ATP to ribulose 1,5-bisphosphate.
response to cold Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cold stimulus, a temperature stimulus below the optimal temperature for that organism.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAFTMRAPAP RATAQSRVTA NRARRSLVVR ADKDKTVVIG LAADSGCGKS TFMRRMTSIF
70 80 90 100 110 120
GGVPKPPAGG NPDSNTLISD MTTVICLDDY HCLDRNGRKV KGVTALAPEA QNFDLMYNQV
130 140 150 160 170 180
KALKEGKSVD KPIYNHVSGL IDAPEKIESP PILVIEGLHP FYDKRVAELL DFKIYLDISD
190 200 210 220 230 240
DIKFAWKIQR DMAERGHSLE SIKSSIAARK PDFDAYIDPQ KKDADMIIQV LPTQLVPDDK
250 260 270 280 290 300
GQYLRVRLIM KEGSKMFDPV YLFDEGSTIS WIPCGRKLTC SFPGIKMFYG PDTWYGQEVS
310 320 330 340 350 360
VLEMDGQFDK LEELIYVESH LSNTSAKFYG EITQQMLKNS GFPGSNNGTG LFQTIVGLKV
370
REVYERIVKK DVVPV