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 P45119

Entry ID Method Resolution Chain Position Source
AF-P45119-F1 Predicted AlphaFoldDB

No variants for P45119

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P45119

No associated diseases with P45119

3 regional properties for P45119

Type Name Position InterPro Accession
domain Transketolase, N-terminal 104 - 300 IPR005474
domain Pyruvate dehydrogenase E1 component, N-terminal 76 - 458 IPR035807
domain Pyruvate dehydrogenase E1 component, middle domain 487 - 697 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

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

1 GO annotations of molecular function

Name Definition
pyruvate dehydrogenase (acetyl-transferring) activity Catalysis of the reaction: pyruvate + lipoamide = S-acetyldihydrolipoamide + CO2.

1 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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSEILKNDVD PIETQDWLQS LDSLIREEGV ERAQYIVEQV IGQARTSGVS LPTGVTTDYV
70 80 90 100 110 120
NTIPVAEQPA YPGDHAIERR IRSAVRWNAI AMVLRSQKKD LDLGGHISTF QSAATMYEVC
130 140 150 160 170 180
YNHFFKAATE KNGGDLIFFQ GHAAPGMYAR AFLEGRLTEE QMDNFRQEAF TDGLSSYPHP
190 200 210 220 230 240
KLMPEFWQFS TVSMGLGPVN AIYQARFLKY LDNRGLKDTK DQKVYAFLGD GEMDEIESKG
250 260 270 280 290 300
ALTFAAREHL DNLIFTISCN LQRLDGPVNG NGKIVQELEG LFTGAGWEVI KVLWGSDWDK
310 320 330 340 350 360
LFAKDTSGKL TQLMMEVVDG DYLTFKSKDG AYIREHFFGR YPETAALVAD MTDDEIWALR
370 380 390 400 410 420
RGAHDSEKLY AAYAKAQNAT KPVVILAHQV KGYKIPEAES KNTAHQSKKM SYESLKGFRD
430 440 450 460 470 480
FFELPLTDEQ VEKLEYIKFA EGTPEYEYLH GHRKALNGYV PARRTKFDVE YKVPALEEFK
490 500 510 520 530 540
ALLEEQPRGI STTMAFTRAL NILLKDKNIG KTIVPMIADE ARTFGMEGLF RQVGIYNPHG
550 560 570 580 590 600
QNYIPSDRDL VAYYREAKDG QVLQEGINEL GATASWLAAA NSYSVNNQPM IPFFIYYSMF
610 620 630 640 650 660
GFQRVGDMMW AAGDQLARGF MVGGTSGRTT LNGEGLQHED GHSHIQAGII PNCITYDPSF
670 680 690 700 710 720
AFEVAVIMQD GINRMYGEKQ EDVFYYMTTL NEVMDQPAMP AGAEEGIRKG LYKFETVEGK
730 740 750 760 770 780
KGKGHVQLLG SGAIMRHVRE AAQILANDYG VTSDVFSAPS FNELAREGHD AARWNLLHPT
790 800 810 820 830 840
ETQRVPYVAQ VLADLPTVAS TDYVKGYADQ IRAFVPSKHY HVLGTDGFGR SDSRANLREH
850 860 870 880
FEVDARYVVV AALSQLAKEG TVSNQVVADA IAKFGLNVDR INPLYA