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Reviewed, UniProtKB/Swiss-Prot P0AFG4 (ODO1_ECOL6)

Last modified November 25, 2008. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    2-oxoglutarate dehydrogenase E1 component
    EC=1.2.4.2
Alternative name(s):
    Alpha-ketoglutarate dehydrogenase
Gene names
Name: sucA
Ordered Locus Names: c0803
OrganismEscherichia coli O6 [Complete proteome] [HAMAP]
Taxonomic identifier217992 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length933 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

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

Catalytic activity

2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO(2).

Cofactor

Thiamine pyrophosphate By similarity.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the alpha-ketoglutarate dehydrogenase family.

Ontologies

Keywords

   Biological processGlycolysis
   LigandThiamine pyrophosphate
   Molecular functionOxidoreductase
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processglycolysis

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionoxoglutarate dehydrogenase (succinyl-transferring) activity

Inferred from electronic annotation. Source: InterPro

thiamin pyrophosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 9339332-oxoglutarate dehydrogenase E1 component
PRO_0000162193

Sequences

Sequence LengthMass (Da)Tools
P0AFG4-1 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: EAEF8429EC31E749

FASTA933105,062
        10         20         30         40         50         60 
MQNSALKAWL DSSYLSGANQ SWIEQLYEDF LTDPDSVDAN WRSTFQQLPG TGVKPDQFHS 

        70         80         90        100        110        120 
QTREYFRRLA KDASRYSSTI SDPDTNVKQV KVLQLINAYR FRGHQHANLD PLGLWQQDKV 

       130        140        150        160        170        180 
ADLDPSFHDL TEADFQETFN VGSFASGKET MKLGELLEAL KQTYCGPIGA EYMHITSTEE 

       190        200        210        220        230        240 
KRWIQQRIES GRATFNSEEK KRFLSELTAA EGLERYLGAK FPGAKRFSLE GGDALIPMLK 

       250        260        270        280        290        300 
EMIRHAGNSG TREVVLGMAH RGRLNVLVNV LGKKPQDLFD EFAGKHKEHL GTGDVKYHMG 

       310        320        330        340        350        360 
FSSDFQTDGG LVHLALAFNP SHLEIVSPVV IGSVRARLDR LDEPSSNKVL PITIHGDAAV 

       370        380        390        400        410        420 
TGQGVVQETL NMSKARGYEV GGTVRIVINN QVGFTTSNPL DARSTPYCTD IGKMVQAPIF 

       430        440        450        460        470        480 
HVNADDPEAV AFVTRLALDF RNTFKRDVFI DLVCYRRHGH NEADEPSATQ PLMYQKIKKH 

       490        500        510        520        530        540 
PTPRKIYADK LEQEKVATLE DATEMVNLYR DALDAGDCVV AEWRPMNMHS FTWSPYLNHE 

       550        560        570        580        590        600 
WDEEYPNKVE MKRLQELAKR ISTVPEAVEM QSRVAKIYGD RQAMAAGEKL FDWGGAENLA 

       610        620        630        640        650        660 
YATLVDEGIP VRLSGEDSGR GTFFHRHAVI HNQSNGSTYT PLQHIHNGQG AFRVWDSVLS 

       670        680        690        700        710        720 
EEAVLAFEYG YATAEPRTLT IWEAQFGDFA NGAQVVIDQF ISSGEQKWGR MCGLVMLLPH 

       730        740        750        760        770        780 
GYEGQGPEHS SARLERYLQL CAEQNMQVCV PSTPAQVYHM LRRQALRGMR RPLVVMSPKS 

       790        800        810        820        830        840 
LLRHPLAVSS LEELANGTFL PAIGEIDELD PKGVKRVVMC SGKVYYDLLE QRRKNNQHDV 

       850        860        870        880        890        900 
AIVRIEQLYP FPHKAMQEVL QQFAHVKDFV WCQEEPLNQG AWYCSQHHFR EVIPFGASLR 

       910        920        930 
YAGRPASASP AVGYMSVHQK QQQDLVNDAL NVE 

« Hide

References

[1]"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli."
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases

AE014075 Genomic DNA. Translation: AAN79276.1.
RefSeqNP_752733.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1035834.
GenomeReviewsGene locus c0803 in contig AE014075_GR.
KEGGecc:c0803.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP0AFG4.

Family and domain databases

InterProIPR011603. 2oxoglutarate_DHase_E1.
IPR001017. DHase_E1.
IPR005475. Transketo_Cen_R.
[Graphical view]
PANTHERPTHR23152. 2oxoglutarate_DH_E1. 1 hit.
PfamPF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view]
PIRSFPIRSF000157. Oxoglu_dh_E1. 1 hit.
TIGRFAMsTIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNetSearch...

Entry information

Entry nameODO1_ECOL6
AccessionPrimary (citable) accession number: P0AFG4
Secondary accession number(s): P07015, P78225
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: December 20, 2005
Last modified: November 25, 2008
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents