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Protein

2-oxoglutarate dehydrogenase E1 component

Gene

odhA

Organism
Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)
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

BioCyciBCER226900:GJEU-1252-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:odhAUniRule annotation
Ordered Locus Names:BC_1252
OrganismiBacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)
Taxonomic identifieri226900 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000001417 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9559552-oxoglutarate dehydrogenase E1 componentPRO_0000162163Add
BLAST

Proteomic databases

PRIDEiQ81GF2.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi226900.BC1252.

Structurei

3D structure databases

ProteinModelPortaliQ81GF2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the alpha-ketoglutarate dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0567.
KOiK00164.
OMAiEHSNARP.
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.

Q81GF2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRKNTTTNP WAKFHGPNLG YVIEQYDLYV TGAGSVDPEL QELFEIFGAP
60 70 80 90 100
SFQDDVVTGD NTATHFSPQN TGNIEKILKV VQLVEQIRSF GHTLAHINPM
110 120 130 140 150
EDAANGQSLL EKAMSELSDA DLKAIPAKTV WQDAPEGIHT ALDVIHRLKD
160 170 180 190 200
VYTKSLAYEF SHIQDSEERA WLHQMVESNS LRQPLSNKKR TALLKRLTAV
210 220 230 240 250
EGFEQFLHKT FVGQKRFSIE GVDMLVPVLD EIVLEGAKNG VEDVMIGMAH
260 270 280 290 300
RGRLSVLAHV LEKPYSHMFA EFKHAKIEGA VANSGWTGDV KYHLGREQVV
310 320 330 340 350
SNEEVSTRVT LANNPSHLEF VNPVVEGFAR AAQENRKKSG LPDQDTSKSF
360 370 380 390 400
VILVHGDAAF PGQGIVSETL NLSRLNAYQT GGTIHVIANN AVGFTTDSYD
410 420 430 440 450
SRSTKYSSDL AKGFDIPIVH VNADDPEACL AAANLAIQYR MLFKKDFLID
460 470 480 490 500
LIGYRRYGHN EMDDPAVTQP QVYKKIKNHP TVRAIYADQL QAAGVLNADE
510 520 530 540 550
VETITQFTQE QLKSDYAQVP PADTSDATIH VKVPDVVAKG IQPIDTGVEI
560 570 580 590 600
DSLRAINEGL LSWPEGFNVY PKVKKILERR KDALEENGKI EWALAESLAF
610 620 630 640 650
ASILQEGTPI RLTGQDSQRG TFAHRHIVLH DTDTNETYSP LHRLPNINAS
660 670 680 690 700
FSVHNSPLSE AAVVGYEYGY NVFAPETLVM WEAQYGDFSN TAQALFDQYV
710 720 730 740 750
SAGRAKWGQK SGLVLLLPHG YEGQGPEHSS ARPERFLQLA AENNWTVANL
760 770 780 790 800
TSAAQYFHIL RRQASILGTE AVRPLVLMTP KSLLRHPLTL STASQLSEGR
810 820 830 840 850
FQPALEQENL GMKPNKVKRL VLSTGKMAID LAAEIESGKH EYNLDEVHVV
860 870 880 890 900
RIEQLYPFPA EKVQSIIKRF KNLEEIIWVQ EEPRNMGAWH YMAPILFELA
910 920 930 940 950
GDKVKTGYIG RPDRSSPSGG DPFAHKAEQE LIVAHALDVK YNFRQDKQEI

EVYSN
Length:955
Mass (Da):106,412
Last modified:June 1, 2003 - v1
Checksum:i99F267C26CA28433
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016877 Genomic DNA. Translation: AAP08237.1.
RefSeqiNP_831036.1. NC_004722.1.

Genome annotation databases

EnsemblBacteriaiAAP08237; AAP08237; BC_1252.
GeneIDi1203601.
KEGGibce:BC1252.
PATRICi32598227. VBIBacCer54481_1225.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016877 Genomic DNA. Translation: AAP08237.1.
RefSeqiNP_831036.1. NC_004722.1.

3D structure databases

ProteinModelPortaliQ81GF2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi226900.BC1252.

Proteomic databases

PRIDEiQ81GF2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP08237; AAP08237; BC_1252.
GeneIDi1203601.
KEGGibce:BC1252.
PATRICi32598227. VBIBacCer54481_1225.

Phylogenomic databases

eggNOGiCOG0567.
KOiK00164.
OMAiEHSNARP.
OrthoDBiEOG6V1M1F.

Enzyme and pathway databases

BioCyciBCER226900:GJEU-1252-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: ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711.

Entry informationi

Entry nameiODO1_BACCR
AccessioniPrimary (citable) accession number: Q81GF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: June 1, 2003
Last modified: April 29, 2015
This is version 81 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. 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.