Q68EW0

PR
Gene name
ogdhl
Protein name
2-oxoglutarate dehydrogenase-like, mitochondrial
Names
2-oxoglutarate dehydrogenase complex component E1-like, OGDC-E1-like, Alpha-ketoglutarate dehydrogenase-like
Species
Xenopus laevis (African clawed frog)
KEGG Pathway
xla:447370
EC number
1.2.4.2: 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)

1-51 (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 Q68EW0

Entry ID Method Resolution Chain Position Source
AF-Q68EW0-F1 Predicted AlphaFoldDB

No variants for Q68EW0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q68EW0

No associated diseases with Q68EW0

4 regional properties for Q68EW0

Type Name Position InterPro Accession
domain Dehydrogenase, E1 component 252 - 576 IPR001017
domain Transketolase-like, pyrimidine-binding domain 645 - 860 IPR005475
domain Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal 863 - 1008 IPR031717
domain 2-oxoglutarate dehydrogenase E1 component, N-terminal domain 43 - 82 IPR032106

Functions

Description
EC Number 1.2.4.2 With a disulfide as acceptor
Subcellular Localization
  • Mitochondrion matrix
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
mitochondrial matrix The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.

3 GO annotations of molecular function

Name Definition
metal ion binding Binding to a metal ion.
oxoglutarate dehydrogenase (succinyl-transferring) activity Catalysis of the reaction: 2-oxoglutarate + lipoamide = S-succinyldihydrolipoamide + CO2.
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.

3 GO annotations of biological process

Name Definition
2-oxoglutarate metabolic process The chemical reactions and pathways involving oxoglutarate, the dianion of 2-oxoglutaric acid. It is a key constituent of the TCA cycle and a key intermediate in amino-acid metabolism.
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.
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
MSHLRSVAAK LKPYCTGLLV KHNSILRTLP PRCYVYSSGA KEPFLSGTNS SYVEEMYYAW
70 80 90 100 110 120
LENPKSVHKS WDAFFRSADN GTPQCEIQGV PSLADIESKL PSLSSQGLAT APAKAEKIVE
130 140 150 160 170 180
EHLAVQSLIR AYQIRGHHVA QLDPLGILDA DLDSFVPSDL ITTLDKLGFY GLHEGDLDKV
190 200 210 220 230 240
FRLPTTTYIG GTDSTLSLRE IIRRLENSYC QHIGLEFMFI NDVEQCQWIR QKFETPGIMK
250 260 270 280 290 300
FINEEKRTLL ARLIRSTRFE DFLARKWSSE KRFGLEGCEV MIPALKAIID KSSEMGLEYV
310 320 330 340 350 360
ILGMPHRGRL NVLANVIRKD LDQIFCQFDP KLEASDEGSG DVKYHLGMYH ERINRATNKK
370 380 390 400 410 420
ITLSLVANPS HLEAVDPVVQ GKTKAEQFYR GDTEGNKVMS ILVHGDAAFA GQGVVYETFH
430 440 450 460 470 480
LSDLPSYTTN GTIHIVVNNQ IGFTTDPRMA RSSPYPTDVA RVVNAPIFHV NADDPEAVMY
490 500 510 520 530 540
VCSVAAEWRN TFNKDVVVDL VCYRRSGHNE MDEPMFTQPL MYKQIHKQVP VLKKYADKMI
550 560 570 580 590 600
AEGTVTLQEF EEEIAKYDRI CEEAYARSKD KKILNIKHWL DSPWPGFFTL DGEPKSMTCP
610 620 630 640 650 660
PTGIPEDMLS HIGAIASSVP LKDFKIHGGL SRILKSRLEM TNSRTVDWAL AEYMTFGSLL
670 680 690 700 710 720
KEGIHVRLSG QDVERGTFSH RHHVLHDQEV DRWTCVPMNH LWPNQAPYTV CNSSLSEYGV
730 740 750 760 770 780
LGFELGFAMA SPNALVLWEA QFGDFYNTAQ CIIDQFISSG QAKWVRHNGI VLLLPHGMEG
790 800 810 820 830 840
MGPEHSSARP ERFLQMSNDD SDAYPEFTQD FDVSQLFDCN WIVVNCSNPA SYFHVLRRQI
850 860 870 880 890 900
LLPFRKPLII FTPKSLLRHP EAKSSFDDMK TGTNFQRVIP ENGAASHSPQ EVKRVIFCTG
910 920 930 940 950 960
KVYYELVKER HRKGLDSQVA ITRLEQISPF PFDLVKQEAE KYATSELVWC QEEHKNMGYY
970 980 990 1000 1010
DYVKARFLTI LNHARPVWYV GRDPAAAPAT GNKNTHHVEL RRFLDIAFDL EYFEGKPF