SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q63EB1

- ODO1_BACCZ

UniProt

Q63EB1 - ODO1_BACCZ

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
2-oxoglutarate dehydrogenase E1 component
Gene
odhA, BCE33L1152
Organism
Bacillus cereus (strain ZK / E33L)
Status
Reviewed - 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) By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Thiamine pyrophosphate By similarity.UniRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. glycolytic process Source: UniProtKB-KW
  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

BioCyciBCER288681:GHG7-1232-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
2-oxoglutarate dehydrogenase E1 component (EC:1.2.4.2)
Alternative name(s):
Alpha-ketoglutarate dehydrogenase
Gene namesi
Name:odhA
Ordered Locus Names:BCE33L1152
OrganismiBacillus cereus (strain ZK / E33L)
Taxonomic identifieri288681 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000002612: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9559552-oxoglutarate dehydrogenase E1 componentUniRule annotation
PRO_0000162164Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi288681.BCZK1152.

Structurei

3D structure databases

ProteinModelPortaliQ63EB1.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0567.
KOiK00164.
OMAiGHQNANL.
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.

Q63EB1-1 [UniParc]FASTAAdd to Basket

« Hide

MTRKNTTTNP WAKFHGPNLG YVIEQYDLYV TGAGSVDPEL QELFEIFGAP    50
SFQDDVVTGD NTATHFSPQN TGNIEKILKV VQLVEQIRSF GHTLAHINPM 100
EDAANGQSLL ERAMNELSDA DLKAIPAKTV WQDAPEGIHT ALDVIHRLKE 150
VYTQSLAYEF SHIQDSEERA WLHQMVESNS LRQPLSNKKR TALLKRLTAV 200
EGFEQFLHKT FVGQKRFSIE GVDMLVPVLD EIVLEGAKNG VEDVMIGMAH 250
RGRLSVLAHV LEKPYSHMFA EFKHAKIEGA VANSGWTGDV KYHLGREQVV 300
SNEEVSTRVT LANNPSHLEF VNPVVEGFAR AAQENRKKSG LPEQDTSKSF 350
VILVHGDAAF PGQGIVSETL NLSRLNAYQT GGTIHVIANN AVGFTTDSYD 400
SRSTKYSSDL AKGFDIPIVH VNADDPEACL AAANLAIQYR MLFKKDFLID 450
LIGYRRYGHN EMDDPAVTQP QVYKKIKNHP TVRAIYADQL QAAGVLNADE 500
IETITQFTQE QLKSDYAQVP PADTSDATIH VKVPDVVAKG IQPIDTGVEL 550
DSLRAINEGL LSWPEGFNVY PKVKKILERR KDALEENGKI EWALAESLAF 600
ASILQEGTPI RLTGQDSQRG TFAHRHIVLH DTDTNETYSP LHRLPNINAS 650
FSVHNSPLSE AAVVGYEYGY NVFAPETLVM WEAQYGDFSN TAQALFDQYV 700
SAGRAKWGQK SGLVLLLPHG YEGQGPEHSS ARPERFLQLA AENNWTVANL 750
TSAAQYFHIL RRQASILGTE AVRPLVLMTP KSLLRHPLTL STASQLSEGR 800
FQPALEQENL GTKPNKVKRL VLSTGKMAID LAAEIESGKH EYNLDEIHIV 850
RIEQLYPFPA EKVQSIIKRF KNLEEIIWVQ EEPRNMGAWH YMAPILFELA 900
GDKVKTGYIG RPDRSSPSGG DPFAHKAEQE LIVAHALDVK YNFRQDKLEI 950
EVFSN 955
Length:955
Mass (Da):106,476
Last modified:October 25, 2004 - v1
Checksum:i528E7E8C90512B82
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000001 Genomic DNA. Translation: AAU19096.1.
RefSeqiWP_000197164.1. NC_006274.1.
YP_082751.1. NC_006274.1.

Genome annotation databases

EnsemblBacteriaiAAU19096; AAU19096; BCE33L1152.
GeneIDi3026301.
KEGGibcz:BCZK1152.
PATRICi18885744. VBIBacCer95304_1212.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000001 Genomic DNA. Translation: AAU19096.1 .
RefSeqi WP_000197164.1. NC_006274.1.
YP_082751.1. NC_006274.1.

3D structure databases

ProteinModelPortali Q63EB1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 288681.BCZK1152.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAU19096 ; AAU19096 ; BCE33L1152 .
GeneIDi 3026301.
KEGGi bcz:BCZK1152.
PATRICi 18885744. VBIBacCer95304_1212.

Phylogenomic databases

eggNOGi COG0567.
KOi K00164.
OMAi GHQNANL.
OrthoDBi EOG6V1M1F.

Enzyme and pathway databases

BioCyci BCER288681:GHG7-1232-MONOMER.

Family and domain databases

Gene3Di 3.40.50.970. 2 hits.
HAMAPi MF_01169. SucA_OdhA.
InterProi IPR011603. 2oxoglutarate_DH_E1.
IPR023784. 2oxoglutarate_DH_E1_bac.
IPR001017. DH_E1.
IPR029061. THDP-binding.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view ]
PANTHERi PTHR23152. PTHR23152. 1 hit.
Pfami PF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view ]
PIRSFi PIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTi SM00861. Transket_pyr. 1 hit.
[Graphical view ]
SUPFAMi SSF52518. SSF52518. 2 hits.
TIGRFAMsi TIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ZK / E33L.

Entry informationi

Entry nameiODO1_BACCZ
AccessioniPrimary (citable) accession number: Q63EB1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: October 25, 2004
Last modified: September 3, 2014
This is version 67 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi