[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., Kawai S., Ito S., Horikoshi K.; "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-K16."; Submitted (OCT-2003) 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

AP006627; BAD64649.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_175610.1; -.

3D structure databases

ModBase

Q5WG56.

Enzyme and pathway databases

BioCyc

BCLA66692:ABC2114-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

Q5WG56.

Genome annotation databases

GeneID

3202055; -.

GenomeReviews

AP006627_GR; ABC2114.

KEGG

bcl:ABC2114; -.

NMPDR

fig|66692.3.peg.2418; -.

Phylogenomic databases

HOGENOM

Q5WG56; -.

Genome annotation databases

CMR

Q5WG56; ABC2114.

Other

ProtoNet

Q5WG56.

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`	`1 943`	`943`		`2-oxoglutarate dehydrogenase E1 component.`	`PRO_0000162168`

Sequence information

Length: 943 AA [This is the length of the unprocessed precursor]

Molecular weight: 106584 Da [This is the MW of the unprocessed precursor]

CRC64: 3FF67A61E3A2C6D8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSSKEHSPEK PWRGFYGPNL GAVIELYDQY VEDPNSVDEQ TRAHFEKWGP PALEENVSSS 

        70         80         90        100        110        120 
NAKETIGADM ISAVVGAVRL ADYIRAKGHL VSDIQPIWKT DKNSNLLDYD RFNVTEEELK 

       130        140        150        160        170        180 
KVPVKLICKD APPHLKNGLE AIEHLKKVYT QTMAFEFGHV QDEEERNWLR KQVESEAYAD 

       190        200        210        220        230        240 
ELPNKEKKAL LERLTSVEGF EKFIHRTFVG QKRFSIEGLD TLVPMLDKAI REVRKEKTDH 

       250        260        270        280        290        300 
VMIGMAHRGR LNVLAHTLGK PYKAIFSEFL QAPNKLNAPS EGLGETYTGW TGDVKYHLGA 

       310        320        330        340        350        360 
DRQISDDKSA QTIVSLANNP SHLEFVSPIV EGYARAAQED RSSKGAPKQD TTRAYSILIH 

       370        380        390        400        410        420 
GDAAFPGQGV VTETLNLSRL NGYHVGGSLH IIANNNIGYT TEMHDSRSTT YASDPAKGFE 

       430        440        450        460        470        480 
IPIVHVNADD AEACVRAIKF AVEYRRKFQK DFLIDLIGYR RFGHNEGDEP AVTQPDLYAQ 

       490        500        510        520        530        540 
IRKHPTVRAI YAKQLEAEQV ITAKEAQKLD TDMYNYLLEE YNKVNSDKSE KKYELSPPDF 

       550        560        570        580        590        600 
IVDGLPKVKT AVEKEKLVAM NEQLLDWPSS FKPNQKLEKI LKRRANAFDG EGNVDWGLAE 

       610        620        630        640        650        660 
ILAFASILHD GTPVRLSGQD SERGTFAHRH FVLHDRETNE THVPLQTIKD ANASFAVYNS 

       670        680        690        700        710        720 
PLTEQACVGF EYGYNVFSKE TLVLWEAQFG DFVNGAQVMF DQWVSAGRAK WGQKSGLVVL 

       730        740        750        760        770        780 
LPHGYEGAGP EHSSGRVERF LSSAAENNWT VANCTSAAQY FHILRRQAKI LQKNTVRPLI 

       790        800        810        820        830        840 
IMTPKSLLRN QVVASPTSAF TEGEFQPILE EPTLGHDPNA VKRIILCSGK LAIELQDYVN 

       850        860        870        880        890        900 
KNDEDWSWVH IIRVEELYPF PRRAIRERLK EFPNLEEVKW VQEEPKNMGA WTFMEPRIRE 

       910        920        930        940 
ILPSGVPLSY IGRTYRSSPA EGVSNAHKVE QKRIVTESLT RKN

Q5WG56 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