NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DSM 14371 / JCM 11309 / KCTC 3954 / HTE831;
DOI=10.1093/nar/gkf526; PubMed=12235376 [NCBI, ExPASy, EBI, Israel, Japan]
Takami H., Takaki Y., Uchiyama I.;
"Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge and its unexpected adaptive capabilities to extreme environments.";
Nucleic Acids Res. 30:3927-3935(2002).

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 + CO₂.
COFACTOR: Thiamine pyrophosphate (By similarity).
SUBUNIT: Homodimer (By similarity).
SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BA000028; BAC13045.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_692010.1; -.

3D structure databases

ModBase

Q8CUL8.

Enzyme and pathway databases

BioCyc

OIHE221109:OB1089-MON; -.

Ontologies

GO:0004591;	Molecular function: oxoglutarate dehydrogenase (succinyl-transferring) activity (inferred from electronic annotation from HAMAP).
GO:0030976;	Molecular function: thiamin pyrophosphate binding (inferred from electronic annotation from HAMAP).
GO:0006096;	Biological process: glycolysis (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01169; -; 1.
PBIL [Tree]

InterPro

IPR011603; 2oxoglutarate_DHase_E1.
IPR001017; DHase_E1.
IPR005475; Transketo_Cen_R.
Graphical view of domain structure.

PANTHER

PTHR23152; 2oxoglutarate_DH_E1; 1.

Pfam

PF00676; E1_dh; 1.
PF02779; Transket_pyr; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000157; Oxoglu_dh_E1; 1.

TIGRFAMs

TIGR00239; 2oxo_dh_E1; 1.

BLOCKS

Q8CUL8.

Genome annotation databases

1017056; -.

BA000028_GR; OB1089.

oih:OB1089; -.

fig|221109.1.peg.1090; -.

Phylogenomic databases

HOGENOM

Q8CUL8; -.

Genome annotation databases

CMR

Q8CUL8; OB1089.

Other

ProtoNet

Q8CUL8.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Glycolysis; Oxidoreductase; Thiamine pyrophosphate.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 953`	`953`		`2-oxoglutarate dehydrogenase E1 component.`	`PRO_0000162175`

Sequence information

Length: 953 AA [This is the length of the unprocessed precursor]

Molecular weight: 107266 Da [This is the MW of the unprocessed precursor]

CRC64: 78AB32B7CFBE7A6E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAENAESAER FWGQFHGQNT GYLEQQFELY KEDPELVESS IRTIFDTHGA PSWLSSTENV 

        70         80         90        100        110        120 
KSVSNASDFD VTKLTSAIRL VEAIRRYGHT DADIYPVGGY KGDRSKMLDL STYNLKEQDL 

       130        140        150        160        170        180 
EKIPASWIWE KQAPGVATAL DVVNQLKKYY TGTITFEYDH VNNDEERKWL FDLIEEGNAR 

       190        200        210        220        230        240 
LDPSDDERKK ILQRLADVEG FEKFLHKTFV GQKRFSIEGL ESMVPMIDHI VQYSNQDSIE 

       250        260        270        280        290        300 
HVMMGMAHRG RLSVLANVLG KPYDKIFSEF NYTKEKELMP SEGSRAINYG WTGDVKYHYG 

       310        320        330        340        350        360 
AEKEVEFGNK GQTRITLAHN PSHLEFVNPV VEGFTRAAQD DRSEKGYPKQ VTNKAVSVLI 

       370        380        390        400        410        420 
HGDAAFIGEG VVAETLNLSG LPGYSTGGTL HIIANNLLGY TTDREDGRST RYASDLAKGF 

       430        440        450        460        470        480 
EIPVIRVNAD DPISCISAIK IAYEYRQKFQ KDFLIDLVGY RRYGHNEMDE PRTTQPSLYQ 

       490        500        510        520        530        540 
QIDDHPSVAS LFGKGMEEKG ILQEGGFEEV KSAVEKKLTD IYKGMTESEI GEPEAKLMPQ 

       550        560        570        580        590        600 
VLTNGLDQFT TAIDLATLKS INEELLERPE GFKGFKKTER ILQRRKDALE EGNKADWGTG 

       610        620        630        640        650        660 
EALAFASILK EGTPIRLTGQ DTERGTFAHR HIVLHDVETG EKYSPLHGLS DVEASFDVRN 

       670        680        690        700        710        720 
SPLSEAGVLG FEYGYSVQSP DTLVIWEAQF GDFANAGQVI FDQFISSARA KWGEKSNMVL 

       730        740        750        760        770        780 
LLPHGYEGQG PEHSSARLER FLQMAAENNW IVANVTSSAQ LFHILRRQAA MRDRDEARPL 

       790        800        810        820        830        840 
VLMTPKSSLI RHPRMGATAE EFTDGGFLAL RDQPGFEANR EKVTRLVVGS GKMMIDIEEA 

       850        860        870        880        890        900 
MDDSDETYDW LQIKRVEQIY PFPKKALEEE IKQLPNLKEI VWVQEEPKNM GAWNFVDDYL 

       910        920        930        940        950 
RELLNEDQKL KVISRPDRSA PAGGIPTVHK TAQNKIIKQA LNQSEGGKSS AGN

Q8CUL8 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools