NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Garcia E., Richardson P.;
"Complete sequence of chromosome 1 of Ochrobactrum anthropi ATCC 49188.";
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.

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

CP000758; ABS13654.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001369483.1; -.

3D structure databases

ModBase

A6WXF0.

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

A6WXF0.

Genome annotation databases

GeneID

5381023; -.

GenomeReviews

CP000758_GR; Oant_0933.

KEGG

oan:Oant_0933; -.

CMR

A6WXF0; Oant_0933.

Other

ProtoNet

A6WXF0.

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 1001`	`1001`		`2-oxoglutarate dehydrogenase E1 component.`	`PRO_1000065701`

Sequence information

Length: 1001 AA [This is the length of the unprocessed precursor]

Molecular weight: 112439 Da [This is the MW of the unprocessed precursor]

CRC64: FEFF96316C9AC4AB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MARQEQANDV FALTSFLYGG NADYIEELYA KYEDDPNSVD PQWRDFFAKL GDNADDVKKN 

        70         80         90        100        110        120 
AEGASWTRKN WPIAANGELI SALDGNWAEV EKHVTDKLKG KAAKGEAKGA TGAALTSEEI 

       130        140        150        160        170        180 
TQAARDSVRA IMMIRAYRMR GHLHANLDPL GLSEKPNDYN ELEPENYGFT PADYNRKIFI 

       190        200        210        220        230        240 
DNVLGLEYAT VPEMLDILKR TYCGTIGVEF MHISDPAEKA WIQERIEGPD KKVAFTPEGK 

       250        260        270        280        290        300 
KAILSKLIEA EGFEQFIDVK YKGTKRFGLD GGESLIPALE QIVKRGGAMG VKEIIFGMAH 

       310        320        330        340        350        360 
RGRLNVLSQV MGKPHRAIFH EFKGGSYAPD DVEGSGDVKY HLGASSDREF DGNKVHLSLT 

       370        380        390        400        410        420 
ANPSHLEIVN PVVMGKARAK QDLLAGRTRD DMVPLATRAK VLPLLLHGDA AFAGQGVVAE 

       430        440        450        460        470        480 
CLGLSGLKGH RVAGTLHFII NNQIGFTTNP AFSRSSPYPS DVAKMIEAPI FHVNGDDPEA 

       490        500        510        520        530        540 
VVFAAKVATE FRMTFHKPVV IDMFCYRRFG HNEGDEPSFT QPLMYKAIRA HKTTVQLYSD 

       550        560        570        580        590        600 
KLIAEGLIKQ EEIDQMKAQW RENLETEFDA GQSYKPNKAD WLDGAWAGLR TADNADEQRR 

       610        620        630        640        650        660 
GKTAVPMKTL KEIGKKLVEV PKDFHVHRTI QRFLDNRAKM METGEGIDWA TAESLAFGSL 

       670        680        690        700        710        720 
VAEGSPIRLS GQDVERGTFS QRHTVLYDQE TQNRYIPLNN IQKGQAIYEA INSMLSEEAV 

       730        740        750        760        770        780 
LGYEYGYSLS DPRALVLWEA QFGDFANGAQ VVFDQFISSG ERKWLRMSGL VCLLPHGYEG 

       790        800        810        820        830        840 
QGPEHSSARL ERWLQMCAED NMQVANVTTP ANYFHILRRQ MKRDFRKPLI MMTPKSLLRH 

       850        860        870        880        890        900 
KRAVSTLNEL SGESSFHRLL WDDAQYNKDE GIKLQKDAKI RRVVLCSGKV YYDLYEEREK 

       910        920        930        940        950        960 
RGIDDVYLLR VEQLYPFPAK ALINELSRFR HAEMVWCQEE PKNMGAWSFI DPYLEWVLAH 

       970        980        990       1000 
IDAKHQRVRY AGRPAAASPA TGLMSKHLAQ LAAFLEDALG N

A6WXF0 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