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Protein

2-oxoglutarate dehydrogenase E1 component

Gene

sucA

Organism
Brucella abortus (strain 2308)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

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).UniRule annotation

Catalytic activityi

2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2.UniRule annotation

Cofactori

thiamine diphosphateUniRule annotation

GO - Molecular functioni

  1. oxoglutarate dehydrogenase (succinyl-transferring) activity Source: UniProtKB-HAMAP
  2. thiamine pyrophosphate binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. glycolytic process Source: UniProtKB-HAMAP
  2. tricarboxylic acid cycle Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciBABO359391:GKDV-1974-MONOMER.
BMEL359391:GJOQ-1974-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
2-oxoglutarate dehydrogenase E1 componentUniRule annotation (EC:1.2.4.2UniRule annotation)
Alternative name(s):
Alpha-ketoglutarate dehydrogenaseUniRule annotation
Gene namesi
Name:sucAUniRule annotation
Synonyms:odhAUniRule annotation
Ordered Locus Names:BAB1_1923
OrganismiBrucella abortus (strain 2308)
Taxonomic identifieri359391 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
ProteomesiUP000002719: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 100410042-oxoglutarate dehydrogenase E1 componentPRO_1000065698Add
BLAST

Proteomic databases

PRIDEiQ2YLS2.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi359391.BAB1_1923.

Structurei

3D structure databases

ProteinModelPortaliQ2YLS2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the alpha-ketoglutarate dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0567.
HOGENOMiHOG000259586.
KOiK00164.
OMAiQNQGAWF.
OrthoDBiEOG6V1M1F.

Family and domain databases

Gene3Di3.40.50.970. 2 hits.
HAMAPiMF_01169. SucA_OdhA.
InterProiIPR011603. 2oxoglutarate_DH_E1.
IPR023784. 2oxoglutarate_DH_E1_bac.
IPR001017. DH_E1.
IPR029061. THDP-binding.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view]
PANTHERiPTHR23152. PTHR23152. 1 hit.
PfamiPF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view]
PIRSFiPIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00239. 2oxo_dh_E1. 1 hit.

Sequencei

Sequence statusi: Complete.

Q2YLS2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAKQEQAPDR ANDVFALTSF LYGGNADYIE ELYAKYEDDP NSVDPQWRDF
60 70 80 90 100
FAKLGDNADD VKKNAEGPSW TRKNWPIAAN GELVSALDGN WAEVEKHVTD
110 120 130 140 150
KLKGKAAKGE AKGAAGTPLT AEEITQAARD SVRAIMMIRA YRMRGHLHAN
160 170 180 190 200
LDPLGLAEKP NDYNELEPEN YGFTPADYNR KIFIDNVLGL EYATVPEMLD
210 220 230 240 250
ILKRTYCGAI GVEFMHISDP AEKAWIQERI EGPDKKVAFT PEGKKAILSK
260 270 280 290 300
LIEAEGFEQF IDVKYKGTKR FGLDGGESLI PALEQIVKRG GQMGLKEVVL
310 320 330 340 350
GMAHRGRLNV LSQVMGKPHR AIFHEFKGGS YTPDDVEGSG DVKYHLGASS
360 370 380 390 400
DREFDGNKVH LSLTANPSHL EIVNPVVMGK ARAKQDLLVG RTRDDMVPLS
410 420 430 440 450
ERAKVLPLLL HGDAAFAGQG VVAECLGLSG LKGHRVAGTL HFIINNQIGF
460 470 480 490 500
TTNPAFSRSS PYPSDVAKMI EAPIFHVNGD DPEAVVFAAK VATEFRMTFH
510 520 530 540 550
KPVVIDMFCY RRFGHNEGDE PSFTQPLMYK AIRAHKTTVQ LYGEKLIAEG
560 570 580 590 600
LVTQDDIDRM KADWRQKLEG EFEAGQSYKP NKADWLDGAW AGLRTADNAD
610 620 630 640 650
EQRRGKTAVP VKTLKEIGKK LVEVPKDFHV HRTIQRFLDN RAKMMETGEG
660 670 680 690 700
IDWATAESLA FGSLAVEGHP IRLSGQDVER GTFSQRHTVL YDQENQNRYI
710 720 730 740 750
PLNNLQKGQA IYEAINSMLS EEAVLGYEYG YSLSDPRALV LWEAQFGDFA
760 770 780 790 800
NGAQVVFDQF ISSGERKWLR MSGLVCLLPH GFEGQGPEHS SARLERYLQL
810 820 830 840 850
CAEDNMQVAN VTTPANYFHI LRRQMKRDFR KPLIMMTPKS LLRHKRAIST
860 870 880 890 900
LAELSGESSF HRLLWDDARY NKDKGIKLQK DAKIRRVVLC SGKVYYDLYE
910 920 930 940 950
EREKRGIDDV YLLRVEQLYP FPAKALINEL SRFRHAEMVW CQEEPKNMGA
960 970 980 990 1000
WSFIDPYLEW VLAHIDAKHQ RVRYAGRPAA ASPATGLMSK HLAQLAAFLE

DALG
Length:1,004
Mass (Da):112,708
Last modified:February 7, 2006 - v1
Checksum:i262E9AEB383B1247
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM040264 Genomic DNA. Translation: CAJ11879.1.
RefSeqiYP_415263.1. NC_007618.1.

Genome annotation databases

EnsemblBacteriaiCAJ11879; CAJ11879; BAB1_1923.
GeneIDi3788974.
KEGGibmf:BAB1_1923.
PATRICi17846925. VBIBruMel86222_2003.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM040264 Genomic DNA. Translation: CAJ11879.1.
RefSeqiYP_415263.1. NC_007618.1.

3D structure databases

ProteinModelPortaliQ2YLS2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi359391.BAB1_1923.

Proteomic databases

PRIDEiQ2YLS2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAJ11879; CAJ11879; BAB1_1923.
GeneIDi3788974.
KEGGibmf:BAB1_1923.
PATRICi17846925. VBIBruMel86222_2003.

Phylogenomic databases

eggNOGiCOG0567.
HOGENOMiHOG000259586.
KOiK00164.
OMAiQNQGAWF.
OrthoDBiEOG6V1M1F.

Enzyme and pathway databases

BioCyciBABO359391:GKDV-1974-MONOMER.
BMEL359391:GJOQ-1974-MONOMER.

Family and domain databases

Gene3Di3.40.50.970. 2 hits.
HAMAPiMF_01169. SucA_OdhA.
InterProiIPR011603. 2oxoglutarate_DH_E1.
IPR023784. 2oxoglutarate_DH_E1_bac.
IPR001017. DH_E1.
IPR029061. THDP-binding.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view]
PANTHERiPTHR23152. PTHR23152. 1 hit.
PfamiPF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view]
PIRSFiPIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 2308.

Entry informationi

Entry nameiODO1_BRUA2
AccessioniPrimary (citable) accession number: Q2YLS2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 7, 2006
Last modified: February 4, 2015
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Brucella abortus strain 2308
    Brucella abortus (strain 2308): entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.