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P20707 (ODO1_AZOVI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
Synonyms:odhA
OrganismAzotobacter vinelandii
Taxonomic identifier354 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

Protein attributes

Sequence length943 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 activity

2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2.

Cofactor

Thiamine pyrophosphate.

Subunit structure

Homodimer.

Sequence similarities

Belongs to the alpha-ketoglutarate dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 9439432-oxoglutarate dehydrogenase E1 component
PRO_0000162186

Sequences

Sequence LengthMass (Da)Tools
P20707 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: D3F35356D454E2A1

FASTA943105,688
        10         20         30         40         50         60 
MQDSVMQRMW NSAHLSGGNA AYVEELYELY LHDPNAVPEE WRTYFEKLPA EAGTSTDVPH 

        70         80         90        100        110        120 
APVRDQFVLL AKNQRRAQPV ATSSVSTEHE KKQVEVLRLI QAYRTRGHQA SQLDPLGLWQ 

       130        140        150        160        170        180 
RTAPSDLSIT HYGLTNADLD TPFRTGELYI GKEEATLREI LQALQETYCR TIGAEFTHIV 

       190        200        210        220        230        240 
DSEQRNWFAQ RLESVRGRPV YSKEAKSHLL ERLSAAEGLE KYLGTKYPGT KRFGLEGGES 

       250        260        270        280        290        300 
LVPVVDEIIQ RSGSYGTKEV VIGMAHRGRL NLLVNALGKN PRDLFDEFEG KHLVELGSGD 

       310        320        330        340        350        360 
VKYHQGFSSN VMTSGGEVHL AMAFNPSHLE IVSPVVEGSV RARQDRRVDA TGEKVVPISI 

       370        380        390        400        410        420 
HGDSAFAGQG VVMETFQMSQ IRGYKTGGTI HIVVNNQVGF TTSNPVDTRS TEYCTDPAKM 

       430        440        450        460        470        480 
IQAPVLHVNG DDPEAVLFVT QLAVDYRMQF KRDVVIDLVC YRRRGHNEAD EPSGTQPLMY 

       490        500        510        520        530        540 
QKIAKQPTTR ELYADALVKE GSLSQEEVQA KVDEYRTALD NGQHVLKSLV KEPNTELFVD 

       550        560        570        580        590        600 
WTPYLGHAWT ARHDTSFELK TLQELNAKLL QIPEGFVVQR QVAKILEDRG RMGVGAMPIN 

       610        620        630        640        650        660 
WGCAETLAYA TLLKEGHPVR ITGQDVGRGT FSHRHAALHN QKDASRYIPL QNLYEGQPKF 

       670        680        690        700        710        720 
ELYDSFLSEE AVLAFEYGYA TTTPNALVIW EASSGDFANG AQVVIDQFIS SGETKWGALC 

       730        740        750        760        770        780 
GLTMLLPHGY EGQGPEHSSA RLERYLQLCA EQNIQVCVPT TPAQVYHMLR RQVIRPLRKP 

       790        800        810        820        830        840 
LVALTPKSLL RHKSAISTLE DLALGSFHPV LPEVDSLDPK KVERLVLCSG KVYYDLLDKR 

       850        860        870        880        890        900 
HAEGREDIAI VRIEQLYPFP EEELAEVMAP YTNLKHVVWC QEEPMNQGAW YCSQHHMRRV 

       910        920        930        940 
ASAHKKELFL QYAGREASAA PACGYASMHA EQQEKLLQDA FTV 

« Hide

References

[1]"The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 1. Molecular cloning and sequence analysis of the gene encoding the 2-oxoglutarate dehydrogenase component."
Schulze E., Westphal A.H., Hanemaaijer R., de Kok A.
Eur. J. Biochem. 187:229-234(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 2. Molecular cloning and sequence analysis of the gene encoding the succinyltransferase component."
Westphal A.H., de Kok A.
Eur. J. Biochem. 187:235-239(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 909-943.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X52433 Genomic DNA. Translation: CAA36680.1.
X52432 Genomic DNA. Translation: CAA36677.1.
PIRS07776.

3D structure databases

ProteinModelPortalP20707.
SMRP20707. Positions 90-943.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP20707.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP20707.

Family and domain databases

Gene3D3.40.50.970. 2 hits.
InterProIPR011603. 2oxoglutarate_DH_E1.
IPR001017. DH_E1.
IPR029061. THDP-binding.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view]
PANTHERPTHR23152. PTHR23152. 1 hit.
PfamPF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view]
PIRSFPIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMSSF52518. SSF52518. 2 hits.
TIGRFAMsTIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNetSearch...

Entry information

Entry nameODO1_AZOVI
AccessionPrimary (citable) accession number: P20707
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: June 11, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families