[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Embryo, and Spleen; NIH - Xenopus Gene Collection (XGC) project; Submitted (NOV-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).
ENZYME REGULATION: Catabolite repressed (By similarity).
SUBCELLULAR LOCATION: Mitochondrion matrix (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

BC061938; AAH61938.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC073298; AAH73298.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001083614.1; -.

UniGene

Xl.5294

3D structure databases

ModBase

Q6P6Z8.

Ontologies

GO:0005759;	Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.

Family and domain databases

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

Q6P6Z8.

Genome annotation databases

GeneID

399021; -.

KEGG

xla:399021; -.

Phylogenomic databases

HOVERGEN

Q6P6Z8; -.

Other

ProtoNet

Q6P6Z8.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Glycolysis; Mitochondrion; Oxidoreductase; Thiamine pyrophosphate; Transit peptide; Ubl conjugation.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 40`	`40`	`Mitochondrion (Potential).`
`CHAIN`	`41 1021`	`981`	`2-oxoglutarate dehydrogenase E1 component, mitochondrial.`	`PRO_0000310982`
`CROSSLNK`	`533 533`		`Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) (By similarity).`
`CONFLICT`	`115 115`		`S -> A (in Ref. 1; AAH73298).`

Sequence information

Length: 1021 AA [This is the length of the unprocessed precursor]

Molecular weight: 115633 Da [This is the MW of the unprocessed precursor]

CRC64: 1ED25C4DD47277DB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MFNLRTCASK LRPLTASQTI RSLKHNRPAA PRTFQQFRCL STPVAAEPFL SGTNSNYVEE 

        70         80         90        100        110        120 
MYYAWLENPK SVHKSWDIFF RNANAGASPG AAYQSPPSLG SSLSTLTQAQ SLLHSQPNVD 

       130        140        150        160        170        180 
KLVEDHLAVQ SLIRAYQIRG HHVAQLDPLG ILDADLDSCV PADIVTSSDK LGFYGLQESD 

       190        200        210        220        230        240 
LDKVFHLPTT TFIGGNEMAL PLREIIRRLE NAYCQHIGVE FMFINDLEQC QWIRQKFEAP 

       250        260        270        280        290        300 
GIMQFNNEEK RTLLARLVRS TRFEEFLHRK WSSEKRFGLE GCEVLIPALK TIIDKSSGNG 

       310        320        330        340        350        360 
VDYVIMGMPH RGRLNVLANV IRKELEQIFC QFDSKLEATD EGSGDVKYHL GMYHRRINRV 

       370        380        390        400        410        420 
TDRNITLSLV ANPSHLEAAD PVVQGKTKAE QFYCGDTEGK KVMAILLHGD AAFAGQGIVY 

       430        440        450        460        470        480 
ETFHLSDLPS HTTHGTVHVV VNNQIGFTTD PRMARSSPYP TDVARVVNAP IFHVNADDPE 

       490        500        510        520        530        540 
AVMYVCNVAA EWRSTFHKDV VVDLVCYRRN GHNEMDEPMF TQPLMYKQIR KQKAVLQKYA 

       550        560        570        580        590        600 
ETLISQGVVN QLEYEEEISK YDKICEEAFA RSKDEKILHI KHWLDSPWPG FFTLDGQPRS 

       610        620        630        640        650        660 
MTCPSTGLTE EDLTHIGNVA SSVPVEDFMI HGGLSRILKG RGEMVKNRTV DWALAEYMAL 

       670        680        690        700        710        720 
GSLLKEGIHI RLSGQDVERG TFSHRHHVLH DQNVDKRTCI PMNHLWPNQA PYTVCNSSLS 

       730        740        750        760        770        780 
EYGVLGFELG FAMASPNALV LWEAQFGDFH NTAQCIIDQF VCPGQAKWVR QNGIVLLLPH 

       790        800        810        820        830        840 
GMEGMGPEHS SARPERFLQM CNDDPDVWPK ASEDFAVGQL YDCNWIVVNC STPANFFHVI 

       850        860        870        880        890        900 
RRQILLPFRK PLIVFTPKSL LRHPEARSSF DDMLPSTHFQ RIIPEAGPAS QNPEGVKRLI 

       910        920        930        940        950        960 
FCTGKVYYEL TKERSGRDME GDVAIARVEQ LSPFPFDLVE KEVQKYPNAD LVWCQEEHKN 

       970        980        990       1000       1010       1020 
QGYYDYVKPR LRTTIHRTKP VWYAGRDPAA APATGNKKTH LTELRRFLDT AFNLDAFKGH 


F

Q6P6Z8 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