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Protein

2-oxoglutarate dehydrogenase E1 component

Gene

odhA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 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).

Catalytic activityi

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

Cofactori

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

BioCyciBSUB:BSU19370-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
Synonyms:citK
Ordered Locus Names:BSU19370
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU19370. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9449442-oxoglutarate dehydrogenase E1 componentPRO_0000162169Add
BLAST

Proteomic databases

PaxDbiP23129.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi224308.BSU19370.

Structurei

3D structure databases

ProteinModelPortaliP23129.
SMRiP23129. Positions 71-943.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0567.
HOGENOMiHOG000259588.
InParanoidiP23129.
KOiK00164.
OMAiQNQGAWF.
OrthoDBiEOG6V1M1F.
PhylomeDBiP23129.

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.

P23129-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFQNSMKQRM NWEDFYGPNL GYALELYDQY TQDPNSIDPD LKEMFDELGA
60 70 80 90 100
PPSDIKEASG TKEKGRVTAD LIQKIASAVR LAEDIRTYGH LNASVNPLRK
110 120 130 140 150
DEKKSELFPL SDYGLTEEEI KAIPASVICK DAPKNISNGL EAIQYLRNTY
160 170 180 190 200
KRTISFEFDH VHDFKEREWL TRKIESGELF QKNSAEKLSA VLERLTEVEG
210 220 230 240 250
FEQFLHRTFV GQKRFSIEGL DALVPVLDDI IAQSVKSGTT SVNIGMAHRG
260 270 280 290 300
RLNVLAHVLG KPYEIIFSEF QHAPNKDLVP SEGSIGISYG WTGDVKYHLG
310 320 330 340 350
ANRELQDAET KSARITLANN PSHLEFINPI VEGSTRAAQE TRTQSGYPVQ
360 370 380 390 400
DETKSLAILI HGDAAFPGEG IVAETLNLSS LKGYQVGGAI HIIANNMIGF
410 420 430 440 450
TTESAESRST KYASDLAKGY EIPIVHVNAD DPEACLSAVK FAVEYRKTFN
460 470 480 490 500
KDFLIDLIGY RRYGHNEMDE PSTTQPMLYD AVRKHPTVKQ IFAEKLVKEG
510 520 530 540 550
VVTEEVVQNI EKSVTKRIED AYQKVPSKKE HTACEIELPE PVSNGFPDVD
560 570 580 590 600
TSIDFDVLRK LNGELINWPE SFNVFGKLKR ILERRAKAFD DDRKVEWSLA
610 620 630 640 650
ESLAFASILK DGTPIRLTGQ DSERGTFAQR NLVLHDSETG KEFVPLHHLS
660 670 680 690 700
DCSTSFAVHN SPLSEGSVLG FEYGYNVHSP ETLVLWEAQY GDFANAAQVY
710 720 730 740 750
FDQFISAGRA KWGQKSGLVM LLPHGYEGQG PEHSSGRIER FLQLAAENNW
760 770 780 790 800
TVANLTSAAQ YFHILRRQAK MLLREEIRPL VIMTPKSLLR NPNTVSEVQE
810 820 830 840 850
LSESRFQPVY EQSGLSHDYE KVTRLVLSSG KVSIDISDHF NKLEDGKEWL
860 870 880 890 900
HIARIEQLYP FPAKGVKELF AKLPNLKEIV WVQEEPQNMG AWGYISPYLT
910 920 930 940
EIAPEGVSVQ YIGRRRRSSP AEGDPTVHKK EQERIVSDSL TRKN
Length:944
Mass (Da):106,278
Last modified:July 28, 2009 - v3
Checksum:iDCBC7B28C44A9CC2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351N → Y in CAA38576 (PubMed:1508153).Curated
Sequence conflicti110 – 1101L → S in AAC17864 (PubMed:9734814).Curated
Sequence conflicti133 – 1331P → L in AAC17864 (PubMed:9734814).Curated
Sequence conflicti231 – 2311I → T in AAC17864 (PubMed:9734814).Curated
Sequence conflicti275 – 2773NKD → RS in CAA38576 (PubMed:1508153).Curated
Sequence conflicti283 – 31634GSIGI…SARIT → DPLESATDGRGMSNTIWGRI GSFKTLKQNQPALP in CAA38576 (PubMed:1508153).CuratedAdd
BLAST
Sequence conflicti488 – 4947VKQIFAE → SNKFSLK in CAA38576 (PubMed:1508153).Curated
Sequence conflicti520 – 5223DAY → VAI in CAA38576 (PubMed:1508153).Curated
Sequence conflicti554 – 5563DFD → HFH in CAA38576 (PubMed:1508153).Curated
Sequence conflicti567 – 5693NWP → TG in CAA38576 (PubMed:1508153).Curated
Sequence conflicti573 – 58513NVFGK…ILERR → MFSQAKAHFRKT in CAA38576 (PubMed:1508153).CuratedAdd
BLAST
Sequence conflicti837 – 8382SD → DV in AAA22628 (PubMed:2500417).Curated
Sequence conflicti838 – 8381D → V in CAA38576 (PubMed:1508153).Curated
Sequence conflicti927 – 94418VHKKE…LTRKN → EFIKKNRNVLYLIA in CAA38576 (PubMed:1508153).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54805 Genomic DNA. Translation: CAA38576.1.
AL009126 Genomic DNA. Translation: CAB13829.3.
AF026147 Genomic DNA. Translation: AAC17864.1.
M27141 Genomic DNA. Translation: AAA22628.1.
PIRiS25295. A32879.
RefSeqiNP_389819.3. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB13829; CAB13829; BSU19370.
GeneIDi939507.
KEGGibsu:BSU19370.
PATRICi18975725. VBIBacSub10457_2053.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54805 Genomic DNA. Translation: CAA38576.1.
AL009126 Genomic DNA. Translation: CAB13829.3.
AF026147 Genomic DNA. Translation: AAC17864.1.
M27141 Genomic DNA. Translation: AAA22628.1.
PIRiS25295. A32879.
RefSeqiNP_389819.3. NC_000964.3.

3D structure databases

ProteinModelPortaliP23129.
SMRiP23129. Positions 71-943.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU19370.

Proteomic databases

PaxDbiP23129.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13829; CAB13829; BSU19370.
GeneIDi939507.
KEGGibsu:BSU19370.
PATRICi18975725. VBIBacSub10457_2053.

Organism-specific databases

GenoListiBSU19370. [Micado]

Phylogenomic databases

eggNOGiCOG0567.
HOGENOMiHOG000259588.
InParanoidiP23129.
KOiK00164.
OMAiQNQGAWF.
OrthoDBiEOG6V1M1F.
PhylomeDBiP23129.

Enzyme and pathway databases

BioCyciBSUB:BSU19370-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

« Hide 'large scale' publications
  1. "Organization and regulation of the Bacillus subtilis odhAB operon, which encodes two of the subenzymes of the 2-oxoglutarate dehydrogenase complex."
    Resnekov O., Melin L., Carlsson P., Mannerloev M., von Gabain A., Hederstedt L.
    Mol. Gen. Genet. 234:285-296(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "Detecting and analyzing DNA sequencing errors: toward a higher quality of the Bacillus subtilis genome sequence."
    Medigue C., Rose M., Viari A., Danchin A.
    Genome Res. 9:1116-1127(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  4. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
    Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
    Microbiology 155:1758-1775(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  5. "Sequence analysis of the Bacillus subtilis 168 chromosome region between the sspC and odhA loci (184 degrees-180 degrees)."
    Ghim S.-Y., Choi S.-K., Shin B.-S., Jeong Y.-M., Sorokin A., Ehrlich S.D., Park S.-H.
    DNA Res. 5:195-201(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-270.
    Strain: 168.
  6. "Genetic characterization of Bacillus subtilis odhA and odhB, encoding 2-oxoglutarate dehydrogenase and dihydrolipoamide transsuccinylase, respectively."
    Carlsson P., Hederstedt L.
    J. Bacteriol. 171:3667-3672(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 652-944.
    Strain: 168.

Entry informationi

Entry nameiODO1_BACSU
AccessioniPrimary (citable) accession number: P23129
Secondary accession number(s): O68261, Q45642
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: July 28, 2009
Last modified: February 4, 2015
This is version 117 of the entry and version 3 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. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  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.