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Q5RCB8 (ODO1_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2-oxoglutarate dehydrogenase, mitochondrial

EC=1.2.4.2
Alternative name(s):
2-oxoglutarate dehydrogenase complex component E1
Short name=OGDC-E1
Alpha-ketoglutarate dehydrogenase
Gene names
Name:OGDH
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length1023 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. 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.

Sequence similarities

Belongs to the alpha-ketoglutarate dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4040Mitochondrion By similarity
Chain41 – 10239832-oxoglutarate dehydrogenase, mitochondrial
PRO_0000020435

Amino acid modifications

Modified residue741N6-succinyllysine By similarity
Modified residue4011N6-acetyllysine By similarity
Modified residue5641N6-succinyllysine By similarity
Modified residue9701N6-acetyllysine By similarity
Cross-link534Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5RCB8 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: F432EE1D3502977C

FASTA1,023115,922
        10         20         30         40         50         60 
MFHLRTCAAK LRPLTASQTV KTFSQNRPAA ARTFQQIRCY SAPVAAEPFL SGTSSNYVEE 

        70         80         90        100        110        120 
MYCAWLENPK SVHKSWDIFF RNTNAGAPPG TAYQSPLPLS RGSLAAVAHA QSLVEAQPNV 

       130        140        150        160        170        180 
DKLVEDHLAV QSLIRAYQIR GHHVAQLDPL GILDADLDSS VPADIISSTD KLGFYGLDES 

       190        200        210        220        230        240 
DLDKVFHLPT TTFIGGQESA LPLREIIRRL EMAYCQHIGV EFMFINDLEQ CQWIRQKFET 

       250        260        270        280        290        300 
PGIMQFTNEE KRTLLARLVR STRFEEFLQR KWSSEKRFGL EGCEVLIPAL KTIIDKSSEN 

       310        320        330        340        350        360 
GVDYVIMGMP HRGRLNVLAN VIRKELEQIF CQFDSKLEAA DEGSGDVKYH LGMYHRRINR 

       370        380        390        400        410        420 
VTDRNITLSL VANPSHLEAA DPVVMGKTKA EQFYCGDTEG KKVMSILLHG DAAFAGQGIV 

       430        440        450        460        470        480 
YETFHLSDLP SYTTHGTVHV VVNNQIGFTT DPRMARSSPY PTDVARVVNA PIFHVNSDDP 

       490        500        510        520        530        540 
EAVMYVCKVA AEWRSTFHKD VVVDLVCYRR NGHNEMDEPM FTQPLMYKQI RKQKPVLQKY 

       550        560        570        580        590        600 
AELLVSQGVV NQPEYEEEIS KYDKICEEAF ARSKDEKILH IKHWLDSPWP GFFTLDGQPR 

       610        620        630        640        650        660 
SMSCPSTGLT EDILTHIGNV ASSVPVENFT IHGGLSRILK TRGEMVKNRT VDWALAEYMA 

       670        680        690        700        710        720 
FGSLLKEGIH IRLSGQDVER GTFSHRHHVL HDQNVDKRTC IPMNHLWPNQ APYTVCNSSL 

       730        740        750        760        770        780 
SEYGVLGFEL GFAMASPNAL VLWEAQFGDF HNTAQCIIDQ FICPGQAKWV RQNGIVLLLP 

       790        800        810        820        830        840 
HGMEGMGPEH SSARPERFLQ MCNDDPDVLP DLKEANFDIN QLYDCNWVVV NCSTPGNFFH 

       850        860        870        880        890        900 
VLRRQILLPF RKPLIIFTPK SLLRHPEARS SFDEMLPGTH FQRVIPEDGP AAQNPENVKR 

       910        920        930        940        950        960 
LLFCTGKVYY DLTRERKARD MVGQVAITRI EQLSPFPFDL LLKEVQKYPS AELAWCQEEH 

       970        980        990       1000       1010       1020 
KNQGYYDYVK PRLRTTISRA KPVWYAGRDP AAAPATGNKK THLTELQRLL DTAFDLDIFK 


NFS 

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References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR858358 mRNA. Translation: CAH90589.1.
RefSeqNP_001125317.1. NM_001131845.1.

3D structure databases

ProteinModelPortalQ5RCB8.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ5RCB8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100172216.
KEGGpon:100172216.

Organism-specific databases

CTD4967.

Phylogenomic databases

HOVERGENHBG001892.
InParanoidQ5RCB8.
KOK00164.

Family and domain databases

InterProIPR011603. 2oxoglutarate_DH_E1.
IPR001017. DH_E1.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view]
PANTHERPTHR23152. PTHR23152. 1 hit.
PfamPF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view]
PIRSFPIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
TIGRFAMsTIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNetSearch...

Entry information

Entry nameODO1_PONAB
AccessionPrimary (citable) accession number: Q5RCB8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: December 21, 2004
Last modified: March 19, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families