Skip Header

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

B7I0H2

- ODO1_BACC7

UniProt

B7I0H2 - ODO1_BACC7

(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

Organism
Bacillus cereus (strain AH187)
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).UniRule annotation

Catalytic activityi

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

Cofactori

Thiamine pyrophosphate.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

BioCyciBCER405534:GHXM-1382-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:BCAH187_A1418
OrganismiBacillus cereus (strain AH187)
Taxonomic identifieri405534 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000002214: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9559552-oxoglutarate dehydrogenase E1 componentPRO_1000137969Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi405534.BCAH187_A1418.

Family & Domainsi

Sequence similaritiesi

Belongs to the alpha-ketoglutarate dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0567.
HOGENOMiHOG000259588.
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.

B7I0H2-1 [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 EKAMNELSDA DLKAIPAKTV WQDAPEGIHT ALDVIHRLKE
160 170 180 190 200
VYTQTLAYEF SHIQDSEERA WLHQMVESNS LRQPLSNQKR 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 LPEQDTSKSF
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
IETITQFTQE QLKSDYAQVP PADTSDATIH VKVPDVVAKG IQSIDTGVEL
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 EYNLDEIHIV
860 870 880 890 900
RIEQLYPFPA EKVQSIIKRF KNLEEIIWVQ EEPRNMGAWH YMAPILFELA
910 920 930 940 950
GDKVKTGYIG RPDRSSPSGG DPFAHKAEQE LIVSHALDVK YNFRQDKLEI

EVFSN
Length:955
Mass (Da):106,498
Last modified:February 10, 2009 - v1
Checksum:i8E52C6E86A05BD83
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001177 Genomic DNA. Translation: ACJ78150.1.
RefSeqiYP_002337388.1. NC_011658.1.

Genome annotation databases

EnsemblBacteriaiACJ78150; ACJ78150; BCAH187_A1418.
GeneIDi7075527.
KEGGibcr:BCAH187_A1418.
PATRICi18828261. VBIBacCer120511_1605.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001177 Genomic DNA. Translation: ACJ78150.1 .
RefSeqi YP_002337388.1. NC_011658.1.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 405534.BCAH187_A1418.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACJ78150 ; ACJ78150 ; BCAH187_A1418 .
GeneIDi 7075527.
KEGGi bcr:BCAH187_A1418.
PATRICi 18828261. VBIBacCer120511_1605.

Phylogenomic databases

eggNOGi COG0567.
HOGENOMi HOG000259588.
KOi K00164.
OMAi GHQNANL.
OrthoDBi EOG6V1M1F.

Enzyme and pathway databases

BioCyci BCER405534:GHXM-1382-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. "Genome sequence of Bacillus cereus AH187."
    Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B., Okstad O.A., Ravel J., Sutton G.
    Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AH187.

Entry informationi

Entry nameiODO1_BACC7
AccessioniPrimary (citable) accession number: B7I0H2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: October 1, 2014
This is version 40 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