UniProtKB - P0AFG3 (ODO1_ECOLI)
Protein
2-oxoglutarate dehydrogenase E1 component
Gene
sucA
Organism
Escherichia coli (strain K12)
Status
Functioni
E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO2.1 Publication
Miscellaneous
Binds AMP; however it is not clear if the binding is physiologically relevant.1 Publication
Catalytic activityi
- 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase]-(R)-N6-lipoyl-L-lysine + H+ = [dihydrolipoyllysine-residue succinyltransferase]-(R)-N6-(S8-succinyldihydrolipoyl)-L-lysine + CO21 PublicationEC:1.2.4.21 PublicationThis reaction proceeds in the forward1 Publication direction.
Cofactori
thiamine diphosphate1 Publication
Activity regulationi
Inhibited by oxaloacetate.1 Publication
GO - Molecular functioni
- identical protein binding Source: IntAct
- magnesium ion binding Source: EcoCyc
- nucleotide binding Source: UniProtKB-KW
- oxoglutarate dehydrogenase (succinyl-transferring) activity Source: EcoCyc
- thiamine pyrophosphate binding Source: EcoCyc
GO - Biological processi
- tricarboxylic acid cycle Source: GO_Central
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Tricarboxylic acid cycle |
Ligand | Nucleotide-binding, Thiamine pyrophosphate |
Enzyme and pathway databases
BioCyci | EcoCyc:E1O-MONOMER MetaCyc:E1O-MONOMER |
BRENDAi | 1.2.4.2, 2026 |
SABIO-RKi | P0AFG3 |
Names & Taxonomyi
Protein namesi | Recommended name: 2-oxoglutarate dehydrogenase E1 component (EC:1.2.4.21 Publication)Alternative name(s): Alpha-ketoglutarate dehydrogenase |
Gene namesi | Name:sucA Ordered Locus Names:b0726, JW0715 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytosol
- cytosol Source: EcoCyc
Other locations
- oxoglutarate dehydrogenase complex Source: GO_Central
Pathology & Biotechi
Disruption phenotypei
Impaired growth in minimal medium containing acetate as the sole carbon source.1 Publication
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 260 | H → A: Loss of catalytic activity. 1 Publication | 1 | |
Mutagenesisi | 298 | H → A: Loss of catalytic activity. 1 Publication | 1 | |
Mutagenesisi | 313 | H → A: Mild reduction in growth in presence of acetate or glucose as sole source of carbon; when associated with A-337. 1 Publication | 1 | |
Mutagenesisi | 313 | H → Q: No growth defect in presence of acetate or glucose as sole source of carbon. 1 Publication | 1 | |
Mutagenesisi | 337 | R → A: Mild reduction in growth in presence of acetate or glucose as sole source of carbon; when associated with A-313. 1 Publication | 1 | |
Mutagenesisi | 404 | S → A: No loss of AMPylation by YdiU. 1 Publication | 1 | |
Mutagenesisi | 405 | T → A: Severe reduction in AMPylation by YdiU. 1 Publication | 1 | |
Mutagenesisi | 533 | W → A: Mild reduction in growth in presence of acetate or glucose as sole source of carbon; when associated with A-710. 1 Publication | 1 | |
Mutagenesisi | 533 | W → I: No growth defect in presence of acetate or glucose as sole source of carbon. 1 Publication | 1 | |
Mutagenesisi | 710 | R → A: Mild reduction in growth in presence of acetate or glucose as sole source of carbon; when associated with A-533. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000162191 | 1 – 933 | 2-oxoglutarate dehydrogenase E1 componentAdd BLAST | 933 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 405 | O-AMP-threonine; by ydiU1 Publication | 1 |
Keywords - PTMi
PhosphoproteinProteomic databases
jPOSTi | P0AFG3 |
PaxDbi | P0AFG3 |
PRIDEi | P0AFG3 |
2D gel databases
SWISS-2DPAGEi | P0AFG3 |
Interactioni
Subunit structurei
Homodimer (PubMed:17367808). Part of the 2-oxoglutarate dehydrogenase (OGDH) complex composed of E1 (2-oxoglutarate dehydrogenase), E2 (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide dehydrogenase); the complex contains multiple copies of the three enzymatic components (E1, E2 and E3) (Probable).
Interacts (via N-terminus) with SucB, the E2 component of OGDH complex (PubMed:17367808).
1 Publication1 PublicationBinary interactionsi
Hide detailsP0AFG3
With | #Exp. | IntAct |
---|---|---|
itself | 2 | EBI-543523,EBI-543523 |
sucB [P0AFG6] | 7 | EBI-543523,EBI-558621 |
yheS [P63389] | 3 | EBI-543523,EBI-561198 |
GO - Molecular functioni
- identical protein binding Source: IntAct
Protein-protein interaction databases
BioGRIDi | 849680, 3 interactors |
ComplexPortali | CPX-3921, 2-oxoglutarate dehydrogenase complex |
DIPi | DIP-36225N |
IntActi | P0AFG3, 13 interactors |
MINTi | P0AFG3 |
STRINGi | 511145.b0726 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P0AFG3 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0AFG3 |
Family & Domainsi
Sequence similaritiesi
Belongs to the alpha-ketoglutarate dehydrogenase family.Curated
Phylogenomic databases
eggNOGi | COG0567, Bacteria |
HOGENOMi | CLU_004709_1_0_6 |
InParanoidi | P0AFG3 |
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.
P0AFG3-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 454 | C → S in AAA23897 (PubMed:6376123).Curated | 1 | |
Sequence conflicti | 454 | C → S in CAA25280 (PubMed:6376123).Curated | 1 |
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 |
PIRi | E64808, DEECOG |
RefSeqi | NP_415254.1, NC_000913.3 WP_001181473.1, NZ_STEB01000035.1 |
Genome annotation databases
EnsemblBacteriai | AAC73820; AAC73820; b0726 BAA35392; BAA35392; BAA35392 |
GeneIDi | 57729903 945303 |
KEGGi | ecj:JW0715 eco:b0726 |
PATRICi | fig|1411691.4.peg.1547 |
Similar proteinsi
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 |
PIRi | E64808, DEECOG |
RefSeqi | NP_415254.1, NC_000913.3 WP_001181473.1, NZ_STEB01000035.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2JGD | X-ray | 2.60 | A/B | 1-933 | [»] | |
SMRi | P0AFG3 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 849680, 3 interactors |
ComplexPortali | CPX-3921, 2-oxoglutarate dehydrogenase complex |
DIPi | DIP-36225N |
IntActi | P0AFG3, 13 interactors |
MINTi | P0AFG3 |
STRINGi | 511145.b0726 |
2D gel databases
SWISS-2DPAGEi | P0AFG3 |
Proteomic databases
jPOSTi | P0AFG3 |
PaxDbi | P0AFG3 |
PRIDEi | P0AFG3 |
Genome annotation databases
EnsemblBacteriai | AAC73820; AAC73820; b0726 BAA35392; BAA35392; BAA35392 |
GeneIDi | 57729903 945303 |
KEGGi | ecj:JW0715 eco:b0726 |
PATRICi | fig|1411691.4.peg.1547 |
Organism-specific databases
EchoBASEi | EB0972 |
Phylogenomic databases
eggNOGi | COG0567, Bacteria |
HOGENOMi | CLU_004709_1_0_6 |
InParanoidi | P0AFG3 |
Enzyme and pathway databases
BioCyci | EcoCyc:E1O-MONOMER MetaCyc:E1O-MONOMER |
BRENDAi | 1.2.4.2, 2026 |
SABIO-RKi | P0AFG3 |
Miscellaneous databases
EvolutionaryTracei | P0AFG3 |
PROi | PR:P0AFG3 |
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_ECOLI | |
Accessioni | P0AFG3Primary (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: | April 7, 2021 | |
This is version 128 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families