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Protein

2-oxoglutarate dehydrogenase E1 component

Gene

sucA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).

Catalytic activityi

2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2.

Cofactori

GO - Molecular functioni

  • magnesium ion binding Source: EcoCyc
  • oxoglutarate dehydrogenase (succinyl-transferring) activity Source: EcoCyc
  • thiamine pyrophosphate binding Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciEcoCyc:E1O-MONOMER.
ECOL316407:JW0715-MONOMER.
MetaCyc:E1O-MONOMER.
BRENDAi1.2.4.2. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
2-oxoglutarate dehydrogenase E1 component (EC:1.2.4.2)
Alternative name(s):
Alpha-ketoglutarate dehydrogenase
Gene namesi
Name:sucA
Ordered Locus Names:b0726, JW0715
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10979. sucA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • oxoglutarate dehydrogenase complex Source: GO_Central
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001621911 – 9332-oxoglutarate dehydrogenase E1 componentAdd BLAST933

Proteomic databases

EPDiP0AFG3.
PaxDbiP0AFG3.
PRIDEiP0AFG3.

2D gel databases

SWISS-2DPAGEP0AFG3.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-543523,EBI-543523
sucBP0AFG65EBI-543523,EBI-558621

Protein-protein interaction databases

BioGridi849680. 1 interactor.
DIPiDIP-36225N.
IntActiP0AFG3. 13 interactors.
MINTiMINT-1243484.
STRINGi511145.b0726.

Structurei

Secondary structure

1933
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi85 – 102Combined sources18
Helixi103 – 106Combined sources4
Beta strandi111 – 113Combined sources3
Helixi121 – 123Combined sources3
Helixi126 – 129Combined sources4
Helixi132 – 136Combined sources5
Beta strandi137 – 140Combined sources4
Beta strandi150 – 152Combined sources3
Helixi153 – 165Combined sources13
Beta strandi166 – 171Combined sources6
Helixi178 – 188Combined sources11
Helixi197 – 220Combined sources24
Helixi235 – 247Combined sources13
Turni248 – 250Combined sources3
Beta strandi253 – 257Combined sources5
Helixi263 – 269Combined sources7
Helixi275 – 282Combined sources8
Helixi296 – 298Combined sources3
Beta strandi301 – 307Combined sources7
Beta strandi310 – 316Combined sources7
Beta strandi321 – 324Combined sources4
Helixi326 – 338Combined sources13
Beta strandi341 – 343Combined sources3
Helixi346 – 348Combined sources3
Beta strandi349 – 356Combined sources8
Helixi357 – 362Combined sources6
Helixi365 – 372Combined sources8
Turni376 – 378Combined sources3
Beta strandi384 – 389Combined sources6
Helixi408 – 413Combined sources6
Turni414 – 416Combined sources3
Beta strandi419 – 423Combined sources5
Helixi427 – 444Combined sources18
Beta strandi448 – 453Combined sources6
Helixi474 – 478Combined sources5
Helixi483 – 492Combined sources10
Turni493 – 495Combined sources3
Helixi499 – 515Combined sources17
Helixi528 – 530Combined sources3
Helixi534 – 536Combined sources3
Helixi551 – 560Combined sources10
Helixi572 – 585Combined sources14
Helixi593 – 605Combined sources13
Turni606 – 608Combined sources3
Beta strandi611 – 615Combined sources5
Turni616 – 620Combined sources5
Beta strandi629 – 631Combined sources3
Beta strandi633 – 636Combined sources4
Helixi641 – 643Combined sources3
Beta strandi652 – 655Combined sources4
Helixi661 – 674Combined sources14
Beta strandi678 – 683Combined sources6
Helixi687 – 693Combined sources7
Helixi694 – 699Combined sources6
Turni700 – 703Combined sources4
Helixi704 – 708Combined sources5
Beta strandi715 – 719Combined sources5
Beta strandi723 – 725Combined sources3
Helixi734 – 739Combined sources6
Beta strandi747 – 749Combined sources3
Helixi754 – 766Combined sources13
Beta strandi773 – 777Combined sources5
Helixi780 – 783Combined sources4
Helixi791 – 796Combined sources6
Beta strandi801 – 803Combined sources3
Helixi811 – 813Combined sources3
Beta strandi816 – 820Combined sources5
Helixi824 – 834Combined sources11
Beta strandi839 – 845Combined sources7
Beta strandi847 – 850Combined sources4
Helixi853 – 860Combined sources8
Helixi861 – 863Combined sources3
Beta strandi868 – 876Combined sources9
Beta strandi879 – 881Combined sources3
Helixi882 – 890Combined sources9
Beta strandi898 – 904Combined sources7
Beta strandi908 – 911Combined sources4
Helixi915 – 930Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JGDX-ray2.60A/B1-933[»]
ProteinModelPortaliP0AFG3.
SMRiP0AFG3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AFG3.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C7P. Bacteria.
COG0567. LUCA.
HOGENOMiHOG000259587.
InParanoidiP0AFG3.
KOiK00164.
OMAiQNQGAWF.

Family and domain databases

Gene3Di3.40.50.970. 2 hits.
InterProiIPR032106. 2-oxogl_dehyd_N.
IPR011603. 2oxoglutarate_DH_E1.
IPR001017. DH_E1.
IPR031717. KGD_C.
IPR029061. THDP-binding.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view]
PANTHERiPTHR23152. PTHR23152. 1 hit.
PfamiPF16078. 2-oxogl_dehyd_N. 1 hit.
PF00676. E1_dh. 1 hit.
PF16870. OxoGdeHyase_C. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view]
PIRSFiPIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00239. 2oxo_dh_E1. 1 hit.

Sequencei

Sequence statusi: Complete.

P0AFG3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQNSALKAWL DSSYLSGANQ SWIEQLYEDF LTDPDSVDAN WRSTFQQLPG
60 70 80 90 100
TGVKPDQFHS QTREYFRRLA KDASRYSSTI SDPDTNVKQV KVLQLINAYR
110 120 130 140 150
FRGHQHANLD PLGLWQQDKV ADLDPSFHDL TEADFQETFN VGSFASGKET
160 170 180 190 200
MKLGELLEAL KQTYCGPIGA EYMHITSTEE KRWIQQRIES GRATFNSEEK
210 220 230 240 250
KRFLSELTAA EGLERYLGAK FPGAKRFSLE GGDALIPMLK EMIRHAGNSG
260 270 280 290 300
TREVVLGMAH RGRLNVLVNV LGKKPQDLFD EFAGKHKEHL GTGDVKYHMG
310 320 330 340 350
FSSDFQTDGG LVHLALAFNP SHLEIVSPVV IGSVRARLDR LDEPSSNKVL
360 370 380 390 400
PITIHGDAAV TGQGVVQETL NMSKARGYEV GGTVRIVINN QVGFTTSNPL
410 420 430 440 450
DARSTPYCTD IGKMVQAPIF HVNADDPEAV AFVTRLALDF RNTFKRDVFI
460 470 480 490 500
DLVCYRRHGH NEADEPSATQ PLMYQKIKKH PTPRKIYADK LEQEKVATLE
510 520 530 540 550
DATEMVNLYR DALDAGDCVV AEWRPMNMHS FTWSPYLNHE WDEEYPNKVE
560 570 580 590 600
MKRLQELAKR ISTVPEAVEM QSRVAKIYGD RQAMAAGEKL FDWGGAENLA
610 620 630 640 650
YATLVDEGIP VRLSGEDSGR GTFFHRHAVI HNQSNGSTYT PLQHIHNGQG
660 670 680 690 700
AFRVWDSVLS EEAVLAFEYG YATAEPRTLT IWEAQFGDFA NGAQVVIDQF
710 720 730 740 750
ISSGEQKWGR MCGLVMLLPH GYEGQGPEHS SARLERYLQL CAEQNMQVCV
760 770 780 790 800
PSTPAQVYHM LRRQALRGMR RPLVVMSPKS LLRHPLAVSS LEELANGTFL
810 820 830 840 850
PAIGEIDELD PKGVKRVVMC SGKVYYDLLE QRRKNNQHDV AIVRIEQLYP
860 870 880 890 900
FPHKAMQEVL QQFAHVKDFV WCQEEPLNQG AWYCSQHHFR EVIPFGASLR
910 920 930
YAGRPASASP AVGYMSVHQK QQQDLVNDAL NVE
Length:933
Mass (Da):105,062
Last modified:December 20, 2005 - v1
Checksum:iEAEF8429EC31E749
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti454C → S in AAA23897 (PubMed:6376123).Curated1
Sequence conflicti454C → S in CAA25280 (PubMed:6376123).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01619 Genomic DNA. Translation: AAA23897.1.
X00661 Genomic DNA. Translation: CAA25280.1.
U00096 Genomic DNA. Translation: AAC73820.1.
AP009048 Genomic DNA. Translation: BAA35392.1.
PIRiE64808. DEECOG.
RefSeqiNP_415254.1. NC_000913.3.
WP_001181473.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73820; AAC73820; b0726.
BAA35392; BAA35392; BAA35392.
GeneIDi945303.
KEGGiecj:JW0715.
eco:b0726.
PATRICi32116647. VBIEscCol129921_0756.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01619 Genomic DNA. Translation: AAA23897.1.
X00661 Genomic DNA. Translation: CAA25280.1.
U00096 Genomic DNA. Translation: AAC73820.1.
AP009048 Genomic DNA. Translation: BAA35392.1.
PIRiE64808. DEECOG.
RefSeqiNP_415254.1. NC_000913.3.
WP_001181473.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JGDX-ray2.60A/B1-933[»]
ProteinModelPortaliP0AFG3.
SMRiP0AFG3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi849680. 1 interactor.
DIPiDIP-36225N.
IntActiP0AFG3. 13 interactors.
MINTiMINT-1243484.
STRINGi511145.b0726.

2D gel databases

SWISS-2DPAGEP0AFG3.

Proteomic databases

EPDiP0AFG3.
PaxDbiP0AFG3.
PRIDEiP0AFG3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73820; AAC73820; b0726.
BAA35392; BAA35392; BAA35392.
GeneIDi945303.
KEGGiecj:JW0715.
eco:b0726.
PATRICi32116647. VBIEscCol129921_0756.

Organism-specific databases

EchoBASEiEB0972.
EcoGeneiEG10979. sucA.

Phylogenomic databases

eggNOGiENOG4105C7P. Bacteria.
COG0567. LUCA.
HOGENOMiHOG000259587.
InParanoidiP0AFG3.
KOiK00164.
OMAiQNQGAWF.

Enzyme and pathway databases

BioCyciEcoCyc:E1O-MONOMER.
ECOL316407:JW0715-MONOMER.
MetaCyc:E1O-MONOMER.
BRENDAi1.2.4.2. 2026.

Miscellaneous databases

EvolutionaryTraceiP0AFG3.
PROiP0AFG3.

Family and domain databases

Gene3Di3.40.50.970. 2 hits.
InterProiIPR032106. 2-oxogl_dehyd_N.
IPR011603. 2oxoglutarate_DH_E1.
IPR001017. DH_E1.
IPR031717. KGD_C.
IPR029061. THDP-binding.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view]
PANTHERiPTHR23152. PTHR23152. 1 hit.
PfamiPF16078. 2-oxogl_dehyd_N. 1 hit.
PF00676. E1_dh. 1 hit.
PF16870. OxoGdeHyase_C. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view]
PIRSFiPIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiODO1_ECOLI
AccessioniPrimary (citable) accession number: P0AFG3
Secondary accession number(s): P07015, P78225
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: December 20, 2005
Last modified: November 2, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.