P0AFG8

PR
Gene name
aceE (b0114, JW0110)
Protein name
Pyruvate dehydrogenase E1 component
Names
PDH E1 component
Species
Escherichia coli (strain K12)
KEGG Pathway
eco:b0114
EC number
1.2.4.1: With a disulfide as acceptor
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

429-522 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

9 structures for P0AFG8

Entry ID Method Resolution Chain Position Source
1L8A X-ray 185 A A/B 2-887 PDB
1RP7 X-ray 209 A A/B 2-887 PDB
2G25 X-ray 210 A A/B 2-887 PDB
2G28 X-ray 185 A A/B 2-887 PDB
2G67 X-ray 232 A A/B 2-887 PDB
2IEA X-ray 185 A A/B 2-887 PDB
2QTA X-ray 185 A A/B 2-887 PDB
2QTC X-ray 177 A A/B 2-887 PDB
AF-P0AFG8-F1 Predicted AlphaFoldDB

No variants for P0AFG8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P0AFG8

No associated diseases with P0AFG8

3 regional properties for P0AFG8

Type Name Position InterPro Accession
domain Transketolase, N-terminal 106 - 296 IPR005474
domain Pyruvate dehydrogenase E1 component, N-terminal 76 - 461 IPR035807
domain Pyruvate dehydrogenase E1 component, middle domain 489 - 700 IPR041621

Functions

Description
EC Number 1.2.4.1 With a disulfide as acceptor
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
cytosolic pyruvate dehydrogenase complex Complex that carries out the oxidative decarboxylation of pyruvate to form acetyl-CoA; comprises subunits possessing three catalytic activities: pyruvate dehydrogenase (E1), dihydrolipoamide S-acetyltransferase (E2), and dihydrolipoamide dehydrogenase (E3). Usually contains fewer subunits than its eukaryotic counterpart; for example, the E. coli complex contains 12 E1 dimers, 8 E2 trimers, and 6 E3 dimers arranged in highly symmetric cubic order.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
pyruvate dehydrogenase complex Complex that carries out the oxidative decarboxylation of pyruvate to form acetyl-CoA; comprises subunits possessing three catalytic activities: pyruvate dehydrogenase (E1), dihydrolipoamide S-acetyltransferase (E2), and dihydrolipoamide dehydrogenase (E3).

8 GO annotations of molecular function

Name Definition
identical protein binding Binding to an identical protein or proteins.
magnesium ion binding Binding to a magnesium (Mg) ion.
molecular adaptor activity The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.
protein homodimerization activity Binding to an identical protein to form a homodimer.
pyruvate dehydrogenase (acetyl-transferring) activity Catalysis of the reaction: pyruvate + lipoamide = S-acetyldihydrolipoamide + CO2.
pyruvate dehydrogenase activity Catalysis of the oxidative decarboxylation of pyruvate.
small molecule binding Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.
thiamine pyrophosphate binding Binding to thiamine pyrophosphate, the diphosphoric ester of thiamine. Acts as a coenzyme of several (de)carboxylases, transketolases, and alpha-oxoacid dehydrogenases.

2 GO annotations of biological process

Name Definition
glycolytic process The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules.
pyruvate catabolic process The chemical reactions and pathways resulting in the breakdown of pyruvate, 2-oxopropanoate.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSERFPNDVD PIETRDWLQA IESVIREEGV ERAQYLIDQL LAEARKGGVN VAAGTGISNY
70 80 90 100 110 120
INTIPVEEQP EYPGNLELER RIRSAIRWNA IMTVLRASKK DLELGGHMAS FQSSATIYDV
130 140 150 160 170 180
CFNHFFRARN EQDGGDLVYF QGHISPGVYA RAFLEGRLTQ EQLDNFRQEV HGNGLSSYPH
190 200 210 220 230 240
PKLMPEFWQF PTVSMGLGPI GAIYQAKFLK YLEHRGLKDT SKQTVYAFLG DGEMDEPESK
250 260 270 280 290 300
GAITIATREK LDNLVFVINC NLQRLDGPVT GNGKIINELE GIFEGAGWNV IKVMWGSRWD
310 320 330 340 350 360
ELLRKDTSGK LIQLMNETVD GDYQTFKSKD GAYVREHFFG KYPETAALVA DWTDEQIWAL
370 380 390 400 410 420
NRGGHDPKKI YAAFKKAQET KGKATVILAH TIKGYGMGDA AEGKNIAHQV KKMNMDGVRH
430 440 450 460 470 480
IRDRFNVPVS DADIEKLPYI TFPEGSEEHT YLHAQRQKLH GYLPSRQPNF TEKLELPSLQ
490 500 510 520 530 540
DFGALLEEQS KEISTTIAFV RALNVMLKNK SIKDRLVPII ADEARTFGME GLFRQIGIYS
550 560 570 580 590 600
PNGQQYTPQD REQVAYYKED EKGQILQEGI NELGAGCSWL AAATSYSTNN LPMIPFYIYY
610 620 630 640 650 660
SMFGFQRIGD LCWAAGDQQA RGFLIGGTSG RTTLNGEGLQ HEDGHSHIQS LTIPNCISYD
670 680 690 700 710 720
PAYAYEVAVI MHDGLERMYG EKQENVYYYI TTLNENYHMP AMPEGAEEGI RKGIYKLETI
730 740 750 760 770 780
EGSKGKVQLL GSGSILRHVR EAAEILAKDY GVGSDVYSVT SFTELARDGQ DCERWNMLHP
790 800 810 820 830 840
LETPRVPYIA QVMNDAPAVA STDYMKLFAE QVRTYVPADD YRVLGTDGFG RSDSRENLRH
850 860 870 880
HFEVDASYVV VAALGELAKR GEIDKKVVAD AIAKFNIDAD KVNPRLA