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

1 structures for O09452

Entry ID Method Resolution Chain Position Source
AF-O09452-F1 Predicted AlphaFoldDB

No variants for O09452

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O09452

No associated diseases with O09452

3 regional properties for O09452

Type Name Position InterPro Accession
domain Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain 49 - 198 IPR020828
domain Glyceraldehyde 3-phosphate dehydrogenase, catalytic domain 203 - 360 IPR020829
active_site Glyceraldehyde 3-phosphate dehydrogenase, active site 196 - 203 IPR020830

Functions

Description
EC Number 1.2.1.59 With NAD(+) or NADP(+) as acceptor
Subcellular Localization
  • Plastid, chloroplast
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 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.

4 GO annotations of molecular function

Name Definition
glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity Catalysis of the reaction: D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH + H+.
glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity Catalysis of the reaction: phosphate + NADP+ + glyceraldehyde-3-phosphate = NADPH + 3-phospho-D-glyceroyl-phosphate.
NAD binding Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
NADP binding Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.

2 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.
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAYFKAVAYL AALASAAAFN PGSSFVPRLN APATQPKAAK MTGPTMQAVP CGINGFGRIG
70 80 90 100 110 120
RLVARIMIKD PETKLLQVNA GSATPDYMAY QFKYDSIHGR YQGDVVVDGD DLVIDGQRVI
130 140 150 160 170 180
TTRARDPKDI GWAKTGVEYL CESTGVFLTA EKAQPHIDAG VKKVIFSAPA KDDSLTVVMG
190 200 210 220 230 240
VNAEDYKGQT DFISCASCTT NGLAPLVKCI NDKWGIEEGL MTTIHAMTAT QAVVDSSSRK
250 260 270 280 290 300
DWRGGRAASG NIIPSSTGAA KAVAKVIPAV KGKLTGMAFR VPTIDVSVVD LTCRLAKDAT
310 320 330 340 350 360
YEEICAEVKR RANGDMKGFL GYTDEPLVST DFETEPISST FDAEAGISLN PRFVKLVAWY
370 380
DNEWGYSNRV KDLMVHVAKV DAKVKA