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ECOLI:ODO1

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) sucA
Protein Name(s) 2-oxoglutarate dehydrogenase E1 component

Alpha-ketoglutarate dehydrogenase

External Links
UniProt P0AFG3
EMBL J01619
X00661
U00096
AP009048
PIR E64808
RefSeq NP_415254.1
YP_489005.1
PDB 2JGD
PDBsum 2JGD
ProteinModelPortal P0AFG3
SMR P0AFG3
BioGrid 849680
DIP DIP-36225N
IntAct P0AFG3
MINT MINT-1243484
STRING 511145.b0726
SWISS-2DPAGE P0AFG3
PaxDb P0AFG3
PRIDE P0AFG3
EnsemblBacteria AAC73820
BAA35392
GeneID 12930950
945303
KEGG ecj:Y75_p0705
eco:b0726
PATRIC 32116647
EchoBASE EB0972
EcoGene EG10979
eggNOG COG0567
HOGENOM HOG000259587
InParanoid P0AFG3
KO K00164
OMA QNQGAWF
OrthoDB EOG6V1M1F
BioCyc EcoCyc:E1O-MONOMER
ECOL316407:JW0715-MONOMER
MetaCyc:E1O-MONOMER
EvolutionaryTrace P0AFG3
PRO PR:P0AFG3
Proteomes UP000000318
UP000000625
Genevestigator P0AFG3
GO GO:0005829
GO:0042802
GO:0004591
GO:0030976
GO:0006096
GO:0006099
Gene3D 3.40.50.970
InterPro IPR011603
IPR001017
IPR029061
IPR005475
PANTHER PTHR23152
Pfam PF00676
PF02779
PIRSF PIRSF000157
SMART SM00861
SUPFAM SSF52518
TIGRFAMs TIGR00239

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004591

oxoglutarate dehydrogenase (succinyl-transferring) activity

ECO:0000270

F

Fig. 1 shows the map for SucA in the E. Coli genome that illustrates the genes it is associated with and subsequent activity.

complete

part_of

GO:0005829

cytosol

PMID:16858726[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0045252

oxoglutarate dehydrogenase complex

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000568360
RGD:1561359
UniProtKB:Q02218

C

Seeded From UniProt

complete

involved_in

GO:0006099

tricarboxylic acid cycle

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000568360
RGD:1561359
UniProtKB:P9WIS5

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10979
PANTHER:PTN000568360

C

Seeded From UniProt

complete

enables

GO:0004591

oxoglutarate dehydrogenase (succinyl-transferring) activity

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10979
PANTHER:PTN000568360
RGD:1561359
UniProtKB:P9WIS5
UniProtKB:Q02218

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:24561554[4]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0AFG3

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:16858726[2]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0AFG3

F

Seeded From UniProt

complete

enables

GO:0030976

thiamine pyrophosphate binding

PMID:17367808[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004591

oxoglutarate dehydrogenase (succinyl-transferring) activity

PMID:17367808[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

PMID:17367808[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004591

oxoglutarate dehydrogenase (succinyl-transferring) activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011603

F

Seeded From UniProt

complete

involved_in

GO:0006099

tricarboxylic acid cycle

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011603

P

Seeded From UniProt

complete

enables

GO:0016624

oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001017

F

Seeded From UniProt

complete

enables

GO:0030976

thiamine pyrophosphate binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011603

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011603

P

Seeded From UniProt

complete

enables

GO:0004591

oxoglutarate dehydrogenase (succinyl-transferring) activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.2.4.2

F

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

involved_in

GO:0006099

tricarboxylic acid cycle

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0816

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Darlison, MG et al. (1984) Nucleotide sequence of the sucA gene encoding the 2-oxoglutarate dehydrogenase of Escherichia coli K12. Eur. J. Biochem. 141 351-9 PubMed GONUTS page
  2. 2.0 2.1 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
  3. 3.0 3.1 3.2 3.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  4. Rajagopala, SV et al. (2014) The binary protein-protein interaction landscape of Escherichia coli. Nat. Biotechnol. 32 285-90 PubMed GONUTS page
  5. 5.0 5.1 5.2 Frank, RA et al. (2007) Crystal structure of the E1 component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex. J. Mol. Biol. 368 639-51 PubMed GONUTS page
  6. Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page