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P23129

- ODO1_BACSU

UniProt

P23129 - ODO1_BACSU

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Protein
2-oxoglutarate dehydrogenase E1 component
Gene
odhA, citK, BSU19370
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - 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).UniRule annotation

Catalytic activityi

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

Cofactori

Thiamine pyrophosphate.

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

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: Chromosome

Organism-specific databases

GenoListiBSU19370. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9449442-oxoglutarate dehydrogenase E1 componentUniRule annotation
PRO_0000162169Add
BLAST

Proteomic databases

PaxDbiP23129.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi224308.BSU19370.

Structurei

3D structure databases

ProteinModelPortaliP23129.
SMRiP23129. Positions 71-943.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0567.
HOGENOMiHOG000259588.
KOiK00164.
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

MFQNSMKQRM NWEDFYGPNL GYALELYDQY TQDPNSIDPD LKEMFDELGA    50
PPSDIKEASG TKEKGRVTAD LIQKIASAVR LAEDIRTYGH LNASVNPLRK 100
DEKKSELFPL SDYGLTEEEI KAIPASVICK DAPKNISNGL EAIQYLRNTY 150
KRTISFEFDH VHDFKEREWL TRKIESGELF QKNSAEKLSA VLERLTEVEG 200
FEQFLHRTFV GQKRFSIEGL DALVPVLDDI IAQSVKSGTT SVNIGMAHRG 250
RLNVLAHVLG KPYEIIFSEF QHAPNKDLVP SEGSIGISYG WTGDVKYHLG 300
ANRELQDAET KSARITLANN PSHLEFINPI VEGSTRAAQE TRTQSGYPVQ 350
DETKSLAILI HGDAAFPGEG IVAETLNLSS LKGYQVGGAI HIIANNMIGF 400
TTESAESRST KYASDLAKGY EIPIVHVNAD DPEACLSAVK FAVEYRKTFN 450
KDFLIDLIGY RRYGHNEMDE PSTTQPMLYD AVRKHPTVKQ IFAEKLVKEG 500
VVTEEVVQNI EKSVTKRIED AYQKVPSKKE HTACEIELPE PVSNGFPDVD 550
TSIDFDVLRK LNGELINWPE SFNVFGKLKR ILERRAKAFD DDRKVEWSLA 600
ESLAFASILK DGTPIRLTGQ DSERGTFAQR NLVLHDSETG KEFVPLHHLS 650
DCSTSFAVHN SPLSEGSVLG FEYGYNVHSP ETLVLWEAQY GDFANAAQVY 700
FDQFISAGRA KWGQKSGLVM LLPHGYEGQG PEHSSGRIER FLQLAAENNW 750
TVANLTSAAQ YFHILRRQAK MLLREEIRPL VIMTPKSLLR NPNTVSEVQE 800
LSESRFQPVY EQSGLSHDYE KVTRLVLSSG KVSIDISDHF NKLEDGKEWL 850
HIARIEQLYP FPAKGVKELF AKLPNLKEIV WVQEEPQNMG AWGYISPYLT 900
EIAPEGVSVQ YIGRRRRSSP AEGDPTVHKK EQERIVSDSL TRKN 944
Length:944
Mass (Da):106,278
Last modified:July 28, 2009 - v3
Checksum:iDCBC7B28C44A9CC2
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351N → Y in CAA38576. 1 Publication
Sequence conflicti110 – 1101L → S in AAC17864. 1 Publication
Sequence conflicti133 – 1331P → L in AAC17864. 1 Publication
Sequence conflicti231 – 2311I → T in AAC17864. 1 Publication
Sequence conflicti275 – 2773NKD → RS in CAA38576. 1 Publication
Sequence conflicti283 – 31634GSIGI…SARIT → DPLESATDGRGMSNTIWGRI GSFKTLKQNQPALP in CAA38576. 1 Publication
Add
BLAST
Sequence conflicti488 – 4947VKQIFAE → SNKFSLK in CAA38576. 1 Publication
Sequence conflicti520 – 5223DAY → VAI in CAA38576. 1 Publication
Sequence conflicti554 – 5563DFD → HFH in CAA38576. 1 Publication
Sequence conflicti567 – 5693NWP → TG in CAA38576. 1 Publication
Sequence conflicti573 – 58513NVFGK…ILERR → MFSQAKAHFRKT in CAA38576. 1 Publication
Add
BLAST
Sequence conflicti837 – 8382SD → DV in AAA22628. 1 Publication
Sequence conflicti838 – 8381D → V in CAA38576. 1 Publication
Sequence conflicti927 – 94418VHKKE…LTRKN → EFIKKNRNVLYLIA in CAA38576. 1 Publication
Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi S25295. A32879.
RefSeqi NP_389819.3. NC_000964.3.

3D structure databases

ProteinModelPortali P23129.
SMRi P23129. Positions 71-943.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU19370.

Proteomic databases

PaxDbi P23129.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB13829 ; CAB13829 ; BSU19370 .
GeneIDi 939507.
KEGGi bsu:BSU19370.
PATRICi 18975725. VBIBacSub10457_2053.

Organism-specific databases

GenoListi BSU19370. [Micado ]

Phylogenomic databases

eggNOGi COG0567.
HOGENOMi HOG000259588.
KOi K00164.
OrthoDBi EOG6V1M1F.
PhylomeDBi P23129.

Enzyme and pathway databases

BioCyci BSUB:BSU19370-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

« 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(1992) [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(1997) [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(1999) [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(2009) [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(1998) [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(1989) [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: July 9, 2014
This is version 112 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

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