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Q6P6Z8 (ODO1_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 55. 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
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length1021 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
   PTMIsopeptide bond
Ubl conjugation
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

tricarboxylic acid cycle

Inferred from electronic annotation. Source: InterPro

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionoxoglutarate dehydrogenase (succinyl-transferring) activity

Inferred from electronic annotation. Source: UniProtKB-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 – 10219812-oxoglutarate dehydrogenase, mitochondrial
PRO_0000310982

Amino acid modifications

Cross-link533Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Sequence conflict1151S → A in AAH73298. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q6P6Z8 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 1ED25C4DD47277DB

FASTA1,021115,633
        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 

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References

[1]NIH - Xenopus Gene Collection (XGC) project
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo and Spleen.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC061938 mRNA. Translation: AAH61938.1.
BC073298 mRNA. Translation: AAH73298.1.
RefSeqNP_001083614.1. NM_001090145.1.
UniGeneXl.5294.

3D structure databases

ProteinModelPortalQ6P6Z8.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ6P6Z8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID399021.
KEGGxla:399021.

Organism-specific databases

CTD4967.
XenbaseXB-GENE-1010765. ogdh.

Phylogenomic databases

HOVERGENHBG001892.
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_XENLA
AccessionPrimary (citable) accession number: Q6P6Z8
Secondary accession number(s): Q6GP46
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: July 5, 2004
Last modified: October 16, 2013
This is version 55 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