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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

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

P0AFG3-1 [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)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:
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.
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:
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.
YP_489005.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 85 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