NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1159/000079829; PubMed=15383718 [NCBI, ExPASy, EBI, Israel, Japan]
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential.";
J. Mol. Microbiol. Biotechnol. 7:204-211(2004).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1186/gb-2004-5-10-r77; PubMed=15461803 [NCBI, ExPASy, EBI, Israel, Japan]
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species.";
Genome Biol. 5:RESEARCH077.1-RESEARCH077.12(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

AE017333; AAU41140.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000002; AAU23783.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_079421.1; -.
YP_091833.1; -.

3D structure databases

ModBase

Q65IH4.

Enzyme and pathway databases

BioCyc

BLIC279010:BL01452-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

Q65IH4.

Genome annotation databases

GeneID

3028258; -.
3100388; -.

GenomeReviews

CP000002_GR; BL01452.
AE017333_GR; BLi02260.

KEGG

bld:BLi02260; -.
bli:BL01452; -.

NMPDR

fig|279010.5.peg.30; -.

Phylogenomic databases

HOGENOM

Q65IH4; -.

Genome annotation databases

CMR

Q65IH4; BLi02260.

Other

ProtoNet

Q65IH4.

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`	`1 944`	`944`		`2-oxoglutarate dehydrogenase E1 component.`	`PRO_0000162167`

Sequence information

Length: 944 AA [This is the length of the unprocessed precursor]

Molecular weight: 106671 Da [This is the MW of the unprocessed precursor]

CRC64: 9E63C701C8847E39 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MFQNSMKQRM TWEEFHGPNL GYVLELYDQY VKDPESLDAD LKEMFDELGA PPGDIRAASQ 

        70         80         90        100        110        120 
KNEEADFTAG SIQKIASAVK LAEDIRTYGH LNASVNPLRK TQEKQELFPL AEYGLTEQDV 

       130        140        150        160        170        180 
KKIPASVICK DAPKEVTNGL EAIQYLRNTY KKSISFEFDH VHIFEERNWL MKKIESGELF 

       190        200        210        220        230        240 
TPKSKEKLVE VLRRLTEVES LEQFLHKTFV GQKRFSIEGL DALVPMLDDI IAKSVSAGTT 

       250        260        270        280        290        300 
NVNIGMAHRG RLNVLAHVLG KPYEIIFSEF QHAPNKDLVP SEGSTGINYG WTGDVKYHLG 

       310        320        330        340        350        360 
ANRQIQDEHT KTARIALANN PSHLEFIDPI VEGSTRAAQE TRTESGYPVQ DVKKSMAILI 

       370        380        390        400        410        420 
HGDAAFPGEG IVAETLNLSQ LKGYQVGGAI HIIANNMIGF TTESNESRST KYASDLAKGF 

       430        440        450        460        470        480 
EIPIVHVNAD DPEACLSAVQ LAVEYRMTFN KDFLIDLIGY RRFGHNEMDE PSATQPMLYD 

       490        500        510        520        530        540 
AVRKHPTVKN IFAEKLIHKG IVDKETVGKI KDAVQKRLEE AYRKVPAKKE DMTHEIVLPE 

       550        560        570        580        590        600 
PVSNGFPDVD TSVDFETLRK INQELVSWPE NFNVFDKLKR ILERRAKAFE DDRKVDWSLA 

       610        620        630        640        650        660 
EAMAFASILK DGTPLRLTGQ DSERGTFAHR NLVLHDSKTG DEFIALHHLA DTKASFAVHN 

       670        680        690        700        710        720 
SPLSEGSVLG FEYGYNVSSP ETMVIWEAQF GDFANAAQVY FDQFISAGRA KWGQKSGLVV 

       730        740        750        760        770        780 
LLPHGYEGQG PEHSSGRTER FLQLAAENNW TVANLTSAAQ YFHILRRQAK MLLREEIRPL 

       790        800        810        820        830        840 
IIMTPKSLLR NPNTVSEVQE LSNSSFKPVY EMSGLSHQYD KVTRLVLSSG KVSIDISDHF 

       850        860        870        880        890        900 
NKMEGEKDWL HIARVEELYP FPAKHIKAIF SKLPNLEEIV WVQEEPQNMG AWNYIEPYLR 

       910        920        930        940 
EVAPKDVKVR YIGRRRRSSP AEGDPTVHKK EQERIVSDSL TRKN

Q65IH4 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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