UniProtKB - Q6P6Z8 (ODO1_XENLA)
Protein
2-oxoglutarate dehydrogenase, mitochondrial
Gene
ogdh
Organism
Xenopus laevis (African clawed frog)
Status
Functioni
2-oxoglutarate dehydrogenase (E1) component of the 2-oxoglutarate dehydrogenase complex (OGDHC), which mediates the decarboxylation of alpha-ketoglutarate. The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion. A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A.By similarity
Catalytic activityi
- 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase]-(R)-N6-lipoyl-L-lysine + H+ = [dihydrolipoyllysine-residue succinyltransferase]-(R)-N6-(S8-succinyldihydrolipoyl)-L-lysine + CO2By similarityEC:1.2.4.2By similarityThis reaction proceeds in the forwardBy similarity direction.
Cofactori
thiamine diphosphateBy similarity
Activity regulationi
Calcium ions and ADP stimulate, whereas ATP and NADH reduce catalytic activity.By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 153 | CalciumBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Calcium bindingi | 153 – 157 | By similarity | 5 |
GO - Molecular functioni
- metal ion binding Source: UniProtKB-KW
- oxoglutarate dehydrogenase (succinyl-transferring) activity Source: UniProtKB
- thiamine pyrophosphate binding Source: UniProtKB
GO - Biological processi
- 2-oxoglutarate metabolic process Source: UniProtKB
- glycolytic process Source: UniProtKB-KW
- histone succinylation Source: UniProtKB
- succinyl-CoA metabolic process Source: UniProtKB
- tricarboxylic acid cycle Source: InterPro
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Glycolysis |
Ligand | Calcium, Metal-binding, Thiamine pyrophosphate |
Enzyme and pathway databases
SABIO-RKi | Q6P6Z8 |
Names & Taxonomyi
Protein namesi | Recommended name: 2-oxoglutarate dehydrogenase, mitochondrial (EC:1.2.4.2By similarity)Alternative name(s): 2-oxoglutarate dehydrogenase complex component E1 Short name: OGDC-E1 Alpha-ketoglutarate dehydrogenase |
Gene namesi | Name:ogdh |
Organismi | Xenopus laevis (African clawed frog) |
Taxonomic identifieri | 8355 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus |
Organism-specific databases
Xenbasei | XB-GENE-1010765, ogdh.S |
Subcellular locationi
Mitochondrion
- Mitochondrion matrix By similarity
Nucleus
- Nucleus By similarity
Note: Mainly localizes in the mitochondrion. A small fraction localizes to the nucleus, where the 2-oxoglutarate dehydrogenase complex is required for histone succinylation.By similarity
Mitochondrion
- mitochondrial matrix Source: UniProtKB-SubCell
- mitochondrion Source: UniProtKB
Nucleus
- nucleus Source: UniProtKB
Other locations
- oxoglutarate dehydrogenase complex Source: UniProtKB
Keywords - Cellular componenti
Mitochondrion, NucleusPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transit peptidei | 1 – 40 | MitochondrionSequence analysisAdd BLAST | 40 | |
ChainiPRO_0000310982 | 41 – 1021 | 2-oxoglutarate dehydrogenase, mitochondrialAdd BLAST | 981 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Cross-linki | 533 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity |
Keywords - PTMi
Isopeptide bond, Ubl conjugationInteractioni
Subunit structurei
The 2-oxoglutarate dehydrogenase complex is composed of OGDH (2-oxoglutarate dehydrogenase; E1), DLST (dihydrolipoamide succinyltransferase; E2) and DLD (dihydrolipoamide dehydrogenase; E3). It contains multiple copies of the three enzymatic components (E1, E2 and E3). In the nucleus, the 2-oxoglutarate dehydrogenase complex associates with kat2a.
By similarityFamily & Domainsi
Sequence similaritiesi
Belongs to the alpha-ketoglutarate dehydrogenase family.Curated
Keywords - Domaini
Transit peptidePhylogenomic databases
OrthoDBi | 134699at2759 |
Family and domain databases
Gene3Di | 3.40.50.11610, 1 hit |
InterProi | View protein in InterPro IPR032106, 2-oxogl_dehyd_N IPR011603, 2oxoglutarate_DH_E1 IPR001017, DH_E1 IPR031717, KGD_C IPR042179, KGD_C_sf IPR029061, THDP-binding IPR005475, Transketolase-like_Pyr-bd |
PANTHERi | PTHR23152, PTHR23152, 1 hit |
Pfami | View protein in Pfam PF16078, 2-oxogl_dehyd_N, 1 hit PF00676, E1_dh, 1 hit PF16870, OxoGdeHyase_C, 1 hit PF02779, Transket_pyr, 1 hit |
PIRSFi | PIRSF000157, Oxoglu_dh_E1, 1 hit |
SMARTi | View protein in SMART SM00861, Transket_pyr, 1 hit |
SUPFAMi | SSF52518, SSF52518, 2 hits |
TIGRFAMsi | TIGR00239, 2oxo_dh_E1, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
Q6P6Z8-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MFNLRTCASK LRPLTASQTI RSLKHNRPAA PRTFQQFRCL STPVAAEPFL
60 70 80 90 100
SGTNSNYVEE MYYAWLENPK SVHKSWDIFF RNANAGASPG AAYQSPPSLG
110 120 130 140 150
SSLSTLTQAQ SLLHSQPNVD KLVEDHLAVQ SLIRAYQIRG HHVAQLDPLG
160 170 180 190 200
ILDADLDSCV PADIVTSSDK LGFYGLQESD LDKVFHLPTT TFIGGNEMAL
210 220 230 240 250
PLREIIRRLE NAYCQHIGVE FMFINDLEQC QWIRQKFEAP GIMQFNNEEK
260 270 280 290 300
RTLLARLVRS TRFEEFLHRK WSSEKRFGLE GCEVLIPALK TIIDKSSGNG
310 320 330 340 350
VDYVIMGMPH RGRLNVLANV IRKELEQIFC QFDSKLEATD EGSGDVKYHL
360 370 380 390 400
GMYHRRINRV TDRNITLSLV ANPSHLEAAD PVVQGKTKAE QFYCGDTEGK
410 420 430 440 450
KVMAILLHGD AAFAGQGIVY ETFHLSDLPS HTTHGTVHVV VNNQIGFTTD
460 470 480 490 500
PRMARSSPYP TDVARVVNAP IFHVNADDPE AVMYVCNVAA EWRSTFHKDV
510 520 530 540 550
VVDLVCYRRN GHNEMDEPMF TQPLMYKQIR KQKAVLQKYA ETLISQGVVN
560 570 580 590 600
QLEYEEEISK YDKICEEAFA RSKDEKILHI KHWLDSPWPG FFTLDGQPRS
610 620 630 640 650
MTCPSTGLTE EDLTHIGNVA SSVPVEDFMI HGGLSRILKG RGEMVKNRTV
660 670 680 690 700
DWALAEYMAL GSLLKEGIHI RLSGQDVERG TFSHRHHVLH DQNVDKRTCI
710 720 730 740 750
PMNHLWPNQA PYTVCNSSLS EYGVLGFELG FAMASPNALV LWEAQFGDFH
760 770 780 790 800
NTAQCIIDQF VCPGQAKWVR QNGIVLLLPH GMEGMGPEHS SARPERFLQM
810 820 830 840 850
CNDDPDVWPK ASEDFAVGQL YDCNWIVVNC STPANFFHVI RRQILLPFRK
860 870 880 890 900
PLIVFTPKSL LRHPEARSSF DDMLPSTHFQ RIIPEAGPAS QNPEGVKRLI
910 920 930 940 950
FCTGKVYYEL TKERSGRDME GDVAIARVEQ LSPFPFDLVE KEVQKYPNAD
960 970 980 990 1000
LVWCQEEHKN QGYYDYVKPR LRTTIHRTKP VWYAGRDPAA APATGNKKTH
1010 1020
LTELRRFLDT AFNLDAFKGH F
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 115 | S → A in AAH73298 (Ref. 1) Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BC061938 mRNA Translation: AAH61938.1 BC073298 mRNA Translation: AAH73298.1 |
RefSeqi | NP_001083614.1, NM_001090145.1 XP_018109665.1, XM_018254176.1 XP_018109666.1, XM_018254177.1 |
Genome annotation databases
GeneIDi | 399021 |
KEGGi | xla:399021 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BC061938 mRNA Translation: AAH61938.1 BC073298 mRNA Translation: AAH73298.1 |
RefSeqi | NP_001083614.1, NM_001090145.1 XP_018109665.1, XM_018254176.1 XP_018109666.1, XM_018254177.1 |
3D structure databases
SMRi | Q6P6Z8 |
ModBasei | Search... |
Genome annotation databases
GeneIDi | 399021 |
KEGGi | xla:399021 |
Organism-specific databases
CTDi | 399021 |
Xenbasei | XB-GENE-1010765, ogdh.S |
Phylogenomic databases
OrthoDBi | 134699at2759 |
Enzyme and pathway databases
SABIO-RKi | Q6P6Z8 |
Family and domain databases
Gene3Di | 3.40.50.11610, 1 hit |
InterProi | View protein in InterPro IPR032106, 2-oxogl_dehyd_N IPR011603, 2oxoglutarate_DH_E1 IPR001017, DH_E1 IPR031717, KGD_C IPR042179, KGD_C_sf IPR029061, THDP-binding IPR005475, Transketolase-like_Pyr-bd |
PANTHERi | PTHR23152, PTHR23152, 1 hit |
Pfami | View protein in Pfam PF16078, 2-oxogl_dehyd_N, 1 hit PF00676, E1_dh, 1 hit PF16870, OxoGdeHyase_C, 1 hit PF02779, Transket_pyr, 1 hit |
PIRSFi | PIRSF000157, Oxoglu_dh_E1, 1 hit |
SMARTi | View protein in SMART SM00861, Transket_pyr, 1 hit |
SUPFAMi | SSF52518, SSF52518, 2 hits |
TIGRFAMsi | TIGR00239, 2oxo_dh_E1, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | ODO1_XENLA | |
Accessioni | Q6P6Z8Primary (citable) accession number: Q6P6Z8 Secondary accession number(s): Q6GP46 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 13, 2007 |
Last sequence update: | July 5, 2004 | |
Last modified: | April 7, 2021 | |
This is version 79 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |