NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=HTA426;
DOI=10.1093/nar/gkh970; PubMed=15576355 [NCBI, ExPASy, EBI, Israel, Japan]
Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H., Matsui S., Uchiyama I.;
"Thermoadaptation trait revealed by the genome sequence of thermophilic Geobacillus kaustophilus.";
Nucleic Acids Res. 32:6292-6303(2004).

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

BA000043; BAD75308.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_146876.1; -.

3D structure databases

ModBase

Q5L172.

Enzyme and pathway databases

BioCyc

GKAU235909:GK1023-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

Q5L172.

Genome annotation databases

3184920; -.

BA000043_GR; GK1023.

gka:GK1023; -.

fig|235909.3.peg.1939; -.

Phylogenomic databases

HOGENOM

Q5L172; -.

Genome annotation databases

CMR

Q5L172; GK1023.

Other

ProtoNet

Q5L172.

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`	`1 950`	`950`		`2-oxoglutarate dehydrogenase E1 component.`	`PRO_0000162172`

Sequence information

Length: 950 AA [This is the length of the unprocessed precursor]

Molecular weight: 107561 Da [This is the MW of the unprocessed precursor]

CRC64: 0A9769B6BB8BC10F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAKQTNYAQP WSQFYGPNLG YVIEMYEQYL DDPNSIDPEL KQLFEQWGAP VLEEPVSPAD 

        70         80         90        100        110        120 
DETAKTHQTF RLPETPTIFS KLVAAVKLAD SIRHYGHLVA DTNPLVKKEK KLRRLELDEY 

       130        140        150        160        170        180 
DLTEEDLKRI PVAFLCPHAP AHVKNGWDAI LHLRKIYTDK IAFEFSQVHN LEERNWLIQQ 

       190        200        210        220        230        240 
IESGAYYPSL ANKERVALLR RLTEVEGFEK FIHRTYVGQK RFSIEGLDSM VPLLDELVRQ 

       250        260        270        280        290        300 
AIEHEIDAVN IGMAHRGRLN VLAHVLGKPY EMIFAEFQHA ESKNFIPSEG SVAITYGWTG 

       310        320        330        340        350        360 
DVKYHLGAAR RLRNQSAHTM RITLANNPSH LEVVNPVVLG YTRAAQEDRT KPGVPVQNTD 

       370        380        390        400        410        420 
ASFAILIHGD AAFPGQGIVA ETLNLSQLRG YTTGGTIHII ANNMIGFTTE SYDSRSTTYA 

       430        440        450        460        470        480 
SDMAKGFEVP IVHVNADDPE ACLAAACLAF AYRQRFKKDF VIDLIGYRRF GHNEMDEPMA 

       490        500        510        520        530        540 
TNPTMYAIIN QHPTVRKLYA QKLMEKGIIT EREVDEMEQE VAERLKIAYE RVPKNEDELD 

       550        560        570        580        590        600 
FIMDPPKPVV DRLPEVKTSV AKDVLHRVNE ELLQFPDGFN VFNKLERILK RRSGVFAQNG 

       610        620        630        640        650        660 
KVDWAHAEIL AFATILQDGV PIRLTGQDSQ RGTFAQRHLV LHDVKTGEEY VPLHHISGAK 

       670        680        690        700        710        720 
ASFVVYNSPL TEAAVLGYEY GYNVYAPETL VLWEAQFGDF ANMAQVMFDQ FISSGRAKWG 

       730        740        750        760        770        780 
QKSGLVMLLP HGYEGQGPEH SSGRVERFLQ LAAENNWTVA NLSTAAQYFH ILRRQAALLT 

       790        800        810        820        830        840 
REEVRPLIIM TPKSLLRHPL AASDAEVFVD GAFSPVLEQP GLGADAGKVE RIVFGTGKLM 

       850        860        870        880        890        900 
IDLAEQIGKM ESLDWLHIVR IEELYPFPEE AVKDIIARYP NVKELVWVQE EPKNMGAWLY 

       910        920        930        940        950 
MEPRLRALAP EGVDVSYIGR RRRASPAEGD PVVHRKEQER IIRCALTKHE

Q5L172 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