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P0AFG3

- ODO1_ECOLI

UniProt

P0AFG3 - ODO1_ECOLI

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Protein

2-oxoglutarate dehydrogenase E1 component

Gene

sucA

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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

Thiamine pyrophosphate.

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. oxoglutarate dehydrogenase (succinyl-transferring) activity Source: EcoCyc
  3. thiamine pyrophosphate binding Source: InterPro

GO - Biological processi

  1. glycolytic process Source: UniProtKB-KW
  2. tricarboxylic acid cycle Source: InterPro
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.

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10979. sucA.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9339332-oxoglutarate dehydrogenase E1 componentPRO_0000162191Add
BLAST

Proteomic databases

PaxDbiP0AFG3.
PRIDEiP0AFG3.

2D gel databases

SWISS-2DPAGEP0AFG3.

Expressioni

Gene expression databases

GenevestigatoriP0AFG3.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

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

Protein-protein interaction databases

BioGridi849680. 1 interaction.
DIPiDIP-36225N.
IntActiP0AFG3. 13 interactions.
MINTiMINT-1243484.
STRINGi511145.b0726.

Structurei

Secondary structure

1
933
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi85 – 10218
Helixi103 – 1064
Beta strandi111 – 1133
Helixi121 – 1233
Helixi126 – 1294
Helixi132 – 1365
Beta strandi137 – 1404
Beta strandi150 – 1523
Helixi153 – 16513
Beta strandi166 – 1716
Helixi178 – 18811
Helixi197 – 22024
Helixi235 – 24713
Turni248 – 2503
Beta strandi253 – 2575
Helixi263 – 2697
Helixi275 – 2828
Helixi296 – 2983
Beta strandi301 – 3077
Beta strandi310 – 3167
Beta strandi321 – 3244
Helixi326 – 33813
Beta strandi341 – 3433
Helixi346 – 3483
Beta strandi349 – 3568
Helixi357 – 3626
Helixi365 – 3728
Turni376 – 3783
Beta strandi384 – 3896
Helixi408 – 4136
Turni414 – 4163
Beta strandi419 – 4235
Helixi427 – 44418
Beta strandi448 – 4536
Helixi474 – 4785
Helixi483 – 49210
Turni493 – 4953
Helixi499 – 51517
Helixi528 – 5303
Helixi534 – 5363
Helixi551 – 56010
Helixi572 – 58514
Helixi593 – 60513
Turni606 – 6083
Beta strandi611 – 6155
Turni616 – 6205
Beta strandi629 – 6313
Beta strandi633 – 6364
Helixi641 – 6433
Beta strandi652 – 6554
Helixi661 – 67414
Beta strandi678 – 6836
Helixi687 – 6937
Helixi694 – 6996
Turni700 – 7034
Helixi704 – 7085
Beta strandi715 – 7195
Beta strandi723 – 7253
Helixi734 – 7396
Beta strandi747 – 7493
Helixi754 – 76613
Beta strandi773 – 7775
Helixi780 – 7834
Helixi791 – 7966
Beta strandi801 – 8033
Helixi811 – 8133
Beta strandi816 – 8205
Helixi824 – 83411
Beta strandi839 – 8457
Beta strandi847 – 8504
Helixi853 – 8608
Helixi861 – 8633
Beta strandi868 – 8769
Beta strandi879 – 8813
Helixi882 – 8909
Beta strandi898 – 9047
Beta strandi908 – 9114
Helixi915 – 93016

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JGDX-ray2.60A/B1-933[»]
ProteinModelPortaliP0AFG3.
SMRiP0AFG3. Positions 85-933.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AFG3.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0567.
HOGENOMiHOG000259587.
InParanoidiP0AFG3.
KOiK00164.
OMAiGHQNANL.
OrthoDBiEOG6V1M1F.

Family and domain databases

Gene3Di3.40.50.970. 2 hits.
InterProiIPR011603. 2oxoglutarate_DH_E1.
IPR001017. DH_E1.
IPR029061. THDP-binding.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view]
PANTHERiPTHR23152. PTHR23152. 1 hit.
PfamiPF00676. E1_dh. 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 [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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti454 – 4541C → S in AAA23897. (PubMed:6376123)Curated
Sequence conflicti454 – 4541C → S in CAA25280. (PubMed:6376123)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
YP_489005.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73820; AAC73820; b0726.
BAA35392; BAA35392; BAA35392.
GeneIDi12930950.
945303.
KEGGiecj:Y75_p0705.
eco:b0726.
PATRICi32116647. VBIEscCol129921_0756.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
YP_489005.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2JGD X-ray 2.60 A/B 1-933 [» ]
ProteinModelPortali P0AFG3.
SMRi P0AFG3. Positions 85-933.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 849680. 1 interaction.
DIPi DIP-36225N.
IntActi P0AFG3. 13 interactions.
MINTi MINT-1243484.
STRINGi 511145.b0726.

2D gel databases

SWISS-2DPAGE P0AFG3.

Proteomic databases

PaxDbi P0AFG3.
PRIDEi P0AFG3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73820 ; AAC73820 ; b0726 .
BAA35392 ; BAA35392 ; BAA35392 .
GeneIDi 12930950.
945303.
KEGGi ecj:Y75_p0705.
eco:b0726.
PATRICi 32116647. VBIEscCol129921_0756.

Organism-specific databases

EchoBASEi EB0972.
EcoGenei EG10979. sucA.

Phylogenomic databases

eggNOGi COG0567.
HOGENOMi HOG000259587.
InParanoidi P0AFG3.
KOi K00164.
OMAi GHQNANL.
OrthoDBi EOG6V1M1F.

Enzyme and pathway databases

BioCyci EcoCyc:E1O-MONOMER.
ECOL316407:JW0715-MONOMER.
MetaCyc:E1O-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0AFG3.
PROi P0AFG3.

Gene expression databases

Genevestigatori P0AFG3.

Family and domain databases

Gene3Di 3.40.50.970. 2 hits.
InterProi IPR011603. 2oxoglutarate_DH_E1.
IPR001017. DH_E1.
IPR029061. THDP-binding.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view ]
PANTHERi PTHR23152. PTHR23152. 1 hit.
Pfami PF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view ]
PIRSFi PIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTi SM00861. Transket_pyr. 1 hit.
[Graphical view ]
SUPFAMi SSF52518. SSF52518. 2 hits.
TIGRFAMsi TIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the sucA gene encoding the 2-oxoglutarate dehydrogenase of Escherichia coli K12."
    Darlison M.G., Spencer M.E., Guest J.R.
    Eur. J. Biochem. 141:351-359(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.

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: October 29, 2014
This is version 84 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

External Data

Dasty 3