NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-125 / C-125 / DSM 18197 / FERM 7344 / JCM 9153;
DOI=10.1093/nar/28.21.4317; PubMed=11058132 [NCBI, ExPASy, EBI, Israel, Japan]
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis.";
Nucleic Acids Res. 28:4317-4331(2000).

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

BA000004; BAB05925.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

F83925; F83925.

RefSeq

NP_243072.1; -.

3D structure databases

ModBase

Q9KAT1.

Enzyme and pathway databases

BioCyc

BHAL272558:BH2206-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

Q9KAT1.

Genome annotation databases

891738; -.

BA000004_GR; BH2206.

bha:BH2206; -.

fig|272558.1.peg.2206; -.

Phylogenomic databases

HOGENOM

Q9KAT1; -.

Genome annotation databases

CMR

Q9KAT1; BH2206.

Other

ProtoNet

Q9KAT1.

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`	`1 945`	`945`		`2-oxoglutarate dehydrogenase E1 component.`	`PRO_0000162165`

Sequence information

Length: 945 AA [This is the length of the unprocessed precursor]

Molecular weight: 106970 Da [This is the MW of the unprocessed precursor]

CRC64: DF3D694B15EEAA5C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSSKEHTSEE PWQGFYGPNL GVAVELYEEY QKDPNAVDDE LREAFEKWGP PPATAPERTQ 

        70         80         90        100        110        120 
STFTAASITD PDVIKKFVGA VKLADHIRAF GHLAADIQPI LKEQRREDMF DLDRFGLTES 

       130        140        150        160        170        180 
DIRSVPVDLL CPYAPAHVKN GLDAINHLKE VYTKTIAFEF VHVTDEEERK WLNRMIESGL 

       190        200        210        220        230        240 
YLPNLSTEQR KSLLKRLTDV EGFEKFLHRT FVGQKRFSIE GLDTLVPMLD EVVREAVHEG 

       250        260        270        280        290        300 
TTNVMIGMAH RGRLNVLAHV LNKPYEMIFA EFLHSLNKDL FPSEGSIGIN YGWTGDVKYH 

       310        320        330        340        350        360 
LGADRQIRDE NTAEARLTLA NNPSHLEFVS PIVEGYARAA QEDRTSPGAP EQDIMKAYSI 

       370        380        390        400        410        420 
LIHGDAAFPG QGVVTETLNL SRLTGYQTGG SLHIIANNNI GFTTETFDSR STLYSSDPAK 

       430        440        450        460        470        480 
GFEIPIVHVN ADDPEACLAA VHLAFQYRKR FKKDFLIDLI GYRRFGHNEM DEPAVTQPGV 

       490        500        510        520        530        540 
YQIIRKHPTV RELYSKQLVK KGLIDEQTVK QLDDEVQDKL QSVYEETLRN RTDEHLPDTP 

       550        560        570        580        590        600 
PVEVVNGLPK LDTGVQSETL KAINNELLEW PESFSVNPKL EKILKRRLNV FDGDGKVDWA 

       610        620        630        640        650        660 
LAETLAFATI LHDGTPIRLT GQDSERGTFA HRHLVLHDSR TNDVHSPLQS FRHANASFAV 

       670        680        690        700        710        720 
HNSPLSEMAI VGFEYGYNVF APETLVLWEA QFGDFANGAQ VMFDQWVSAG RAKWGQKSGL 

       730        740        750        760        770        780 
VCLLPHGYEG QGPEHSSARL ERFLVLAAEN NWTIANCTSA AQYFHILRRQ AAILNTDSVR 

       790        800        810        820        830        840 
PLIMMTPKSL LRNQKVASSV EELTTGRFKT VLEQPNLGES HEKVERIVLC SGKIAIDLQD 

       850        860        870        880        890        900 
RIEKEADKDW DWVHIVRVEQ LYPFPKEPLQ EIFARYPNVK EIVWSQEEPR NMGAWPFVQS 

       910        920        930        940 
KIRRAAPNGI NVRYEGRTYR SSPAEGDPII HKQEQERIVT ETLTR

Q9KAT1 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