NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nbt1325; PubMed=17704766 [NCBI, ExPASy, EBI, Israel, Japan]
Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K., Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H., Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H., Strittmatter A., Gottschalk G., Borriss R.;
"Comparative analysis of the complete genome sequence of the plant growth-promoting bacterium Bacillus amyloliquefaciens FZB42.";
Nat. Biotechnol. 25:1007-1014(2007).

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

CP000560; ABS74275.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001421506.1; -.

3D structure databases

ModBase

A7Z5J9.

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

A7Z5J9.

Genome annotation databases

GeneID

5461918; -.

GenomeReviews

CP000560_GR; RBAM_019130.

KEGG

bay:RBAM_019130; -.

CMR

A7Z5J9; RBAM_019130.

Other

ProtoNet

A7Z5J9.

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_1000065696`

Sequence information

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

Molecular weight: 106267 Da [This is the MW of the unprocessed precursor]

CRC64: 936E7315F09C54CD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MFQNNMKQRM NWEDFYGPNL GYALELYDQY AEDPDSIDPD LKDMFDELGA PPSQIKEASG 

        70         80         90        100        110        120 
TKEQGRVTAD LIQKIAAAVK LAEDIRTYGH LNASVNPLRK DPKKSELFPL SDYGLTEEEM 

       130        140        150        160        170        180 
KAIPASVICK DAPANITNGL EAIQHLRNTY KRTISFEFDH VHDFEERAWI TKMVESGELF 

       190        200        210        220        230        240 
RKNSPEKLSA VLERLTEVEG FEQFLHRTFV GQKRFSIEGL DALVPVLDDI IAQSVKAGTT 

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

       310        320        330        340        350        360 
ADRQLQDAET KSARITLANN PSHLEFINPI VEGSTRAAQE TRTQKGYPVQ DETKSLAILI 

       370        380        390        400        410        420 
HGDAAFPGEG IVAETLNLSS LKGYQVGGAI HIIANNMIGF TTESDESRST KYASDLAKGY 

       430        440        450        460        470        480 
EIPIVHVNAD DPEACLSAVK FAVEYRKRFN KDFLIDLIGY RRYGHNEMDE PSTTQPMLYD 

       490        500        510        520        530        540 
AVRKHPTVKR IFAEKLVSEG LISEEKAQNI ETAVTKRIED AYKKVPAKKE DAVREIELPE 

       550        560        570        580        590        600 
PVSNGFPDVD TAIDFDVLRK LNGELINWPE SFNVFGKLKR ILERRAKAFD DDRKVEWSLA 

       610        620        630        640        650        660 
ESLAFASILK DGTPIRLTGQ DSERGTFAQR NLVLHDSETG EEFVALHHLD DCAASFTVHN 

       670        680        690        700        710        720 
SPLSEGSVLG FEYGYNVYSP ETLVMWEAQY GDFANAAQVY FDQFISAGRA KWGQKSGLVM 

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

       790        800        810        820        830        840 
VIMTPKSLLR NPNTVSEVQE LSESRFKPVY EQSGLSHAYE KVTRVVLSSG KVSIDISDHF 

       850        860        870        880        890        900 
NKMEGDKDWL HIARIEQLYP FPAKDTKELF AKLPNLQEIV WVQEEPQNMG AWSYISPYLS 

       910        920        930        940 
EIAPKGVNVQ YIGRRRRSSP AEGDPTVHKK EQERIVSDSL TRKN

A7Z5J9 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