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Q148N0 (ODO1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandThiamine pyrophosphate
   Molecular functionOxidoreductase
   PTMAcetylation
Isopeptide bond
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcerebellar cortex development

Inferred from electronic annotation. Source: Compara

glycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

hippocampus development

Inferred from electronic annotation. Source: Compara

olfactory bulb mitral cell layer development

Inferred from electronic annotation. Source: Compara

pyramidal neuron development

Inferred from electronic annotation. Source: Compara

striatum development

Inferred from electronic annotation. Source: Compara

tangential migration from the subventricular zone to the olfactory bulb

Inferred from electronic annotation. Source: Compara

thalamus development

Inferred from electronic annotation. Source: Compara

tricarboxylic acid cycle

Inferred from electronic annotation. Source: InterPro

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionoxoglutarate dehydrogenase (NAD+) activity

Inferred from electronic annotation. Source: Compara

oxoglutarate dehydrogenase (succinyl-transferring) activity

Inferred from electronic annotation. Source: EC

thiamine pyrophosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4040Mitochondrion Potential
Chain41 – 10239832-oxoglutarate dehydrogenase, mitochondrial
PRO_0000310981

Amino acid modifications

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

Sequences

Sequence LengthMass (Da)Tools
Q148N0 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 46C5D3161D41F551

FASTA1,023115,808
        10         20         30         40         50         60 
MFHLRTCAAK LRPLTASQTV KTFSQNRPAA ARTFGQIRCY TAPVAAEPFL SGTSSNYVEE 

        70         80         90        100        110        120 
MYYAWLENPK SVHKSWDIFF RNTNAGAPPG TAYQSPLPLS PGSLSAVARA GPLVEAQPNV 

       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 
PGVMQFTNEE 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 
SMTCPSTGLT EDILTHIGNV ASSVPVEDFT IHGGLSRILK TRGELVKNRT 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 NFDEMLPGTH FQRVIPEDGP AAQNPGNVKR 

       910        920        930        940        950        960 
LLFCTGKVYY DLTRERKARD MVEQVAITRI EQLSPFPFDL LLQEVQKYPS AELAWCQEEH 

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


NFS

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References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Uterus.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC118106 mRNA. Translation: AAI18107.1.
IPIIPI00687413.
RefSeqNP_001069498.1. NM_001076030.1.
UniGeneBt.46406.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ148N0. 1 interaction.

Proteomic databases

PaxDbQ148N0.
PRIDEQ148N0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000007922; ENSBTAP00000007922; ENSBTAG00000006029.
GeneID534599.
KEGGbta:534599.

Organism-specific databases

CTD4967.

Phylogenomic databases

eggNOGCOG0567.
GeneTreeENSGT00530000063092.
HOGENOMHOG000259586.
HOVERGENHBG001892.
InParanoidQ148N0.
KOK00164.
OMAQEVQKYP.
OrthoDBEOG4VQ9NH.

Enzyme and pathway databases

BioCycCATTLE:534599-MONOMER.

Gene expression databases

ArrayExpressQ148N0.

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...

Other

NextBio20876461.

Entry information

Entry nameODO1_BOVIN
AccessionPrimary (citable) accession number: Q148N0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: August 22, 2006
Last modified: May 29, 2013
This is version 58 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

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