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Protein

2-oxoglutarate dehydrogenase E1 component

Gene

odhA

Organism
Staphylococcus carnosus (strain TM300)
Status
Unreviewed-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
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).SAAS annotation

Catalytic activityi

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

Cofactori

thiamine diphosphateUniRule annotationSAAS annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotationSAAS annotation

Keywords - Biological processi

GlycolysisUniRule annotationSAAS annotation

Keywords - Ligandi

Thiamine pyrophosphateUniRule annotationSAAS annotation

Enzyme and pathway databases

BioCyciSCAR396513:GJ9G-1071-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
2-oxoglutarate dehydrogenase E1 componentUniRule annotationSAAS annotation (EC:1.2.4.2UniRule annotationSAAS annotation)
Alternative name(s):
Alpha-ketoglutarate dehydrogenaseUniRule annotation
Gene namesi
Name:odhAUniRule annotationImported
Ordered Locus Names:Sca_1058Imported
OrganismiStaphylococcus carnosus (strain TM300)Imported
Taxonomic identifieri396513 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000000444 Componenti: Chromosome

Interactioni

Subunit structurei

Homodimer.UniRule annotationSAAS annotation

Protein-protein interaction databases

STRINGi396513.Sca_1058.

Structurei

3D structure databases

ProteinModelPortaliB9DNZ3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the alpha-ketoglutarate dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0567.
HOGENOMiHOG000259588.
KOiK00164.
OMAiNFTQPLM.
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.

B9DNZ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKDKQVSEA PVNFGANLGV IIDLYDQYLQ DPTSVSEDLQ ILFSTINNDN
60 70 80 90 100
REVAASPASS SSDSTIKQVM RLVDNIRQYG HLQSDIYPVN RPERKHVPKL
110 120 130 140 150
TIEDFNLSKD DLEKISPGIV SDHFSDIYDY AYEAIKRMEK RYKGPIAFEY
160 170 180 190 200
THINNNTERT WLKRRIETPY KADLNKNQKI NLFKTLAHVE GFEKYLHKNF
210 220 230 240 250
VGAKRFSIEG VDTLVPMLQE TLRRAAKEEI KNIQIGMAHR GRLNVLTHVL
260 270 280 290 300
EKPYEMMISE FMHTDPMKFL PEDGSLELTS GNAWTSDVKY HLGGIKTTDT
310 320 330 340 350
YGTEQRISLA NNPSHLEIVA PVVLGKTRSV QDDTHEGGKV QTDFSKSMPI
360 370 380 390 400
LIHGDAAYPG QGINFEAMNL GNLDGYSTGG SLHIITNNRI GFTTEARDGR
410 420 430 440 450
STTYSTDVAK GYDIPIMHVN ADNVEATIEA IDIAMDFRKE FNKDVVIDLV
460 470 480 490 500
GYRRYGHNEM DEPSITNPLP YHAIRKHPTV DKIYGEQLVD EGVISKEEME
510 520 530 540 550
QTLDDVQKEL RNSHDKIDKN DKTTTKDMSK PESVEEPLQP DKNNVSYDDL
560 570 580 590 600
KTINDALLTY PTGFEVLKKL NKVLEKRREP FEKEDGLVDW AQAEQLAFAT
610 620 630 640 650
IMQNGTPIRL TGQDSERGTF SHRHAVLHNP DNGDEYVPLQ NVPNQKASFD
660 670 680 690 700
VHNSPLSEAA VVGFEYGYNV ENKGTMNIWE AQYGDFANMA QMMFDNFLFS
710 720 730 740 750
SYAKWGERSG LTLFLPHSYE GQGPEHSSAR LERFLQLSAE NNSTVVNLSS
760 770 780 790 800
SANYYHLLRA QAASLDTDAM RPLVVMSPKS LLRNKTVADT IDKFTEGYFK
810 820 830 840 850
PILPEAHDEK KIKKLILASG KMFIDLKERL QKEPDESILL VAVERLYPFP
860 870 880 890 900
VEEVREVINS LPNLETIAWV QEEPQNQGAW SFVYPYLSDL ASDKYELQYS
910 920 930
GRIKRSAPAE GDGENHKLVQ NSIIEESLNK N
Length:931
Mass (Da):105,560
Last modified:March 24, 2009 - v1
Checksum:i5F7C559FD4DF1E5E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM295250 Genomic DNA. Translation: CAL27966.1.
RefSeqiWP_015900307.1. NC_012121.1.
YP_002634151.1. NC_012121.1.

Genome annotation databases

KEGGisca:Sca_1058.
PATRICi19602884. VBIStaCar105558_1056.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM295250 Genomic DNA. Translation: CAL27966.1.
RefSeqiWP_015900307.1. NC_012121.1.
YP_002634151.1. NC_012121.1.

3D structure databases

ProteinModelPortaliB9DNZ3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi396513.Sca_1058.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGisca:Sca_1058.
PATRICi19602884. VBIStaCar105558_1056.

Phylogenomic databases

eggNOGiCOG0567.
HOGENOMiHOG000259588.
KOiK00164.
OMAiNFTQPLM.
OrthoDBiEOG6V1M1F.

Enzyme and pathway databases

BioCyciSCAR396513:GJ9G-1071-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. "Genome analysis of the meat starter culture bacterium Staphylococcus carnosus TM300."
    Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C., Gotz F.
    Appl. Environ. Microbiol. 75:811-822(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: TM300Imported.

Entry informationi

Entry nameiB9DNZ3_STACT
AccessioniPrimary (citable) accession number: B9DNZ3
Entry historyi
Integrated into UniProtKB/TrEMBL: March 24, 2009
Last sequence update: March 24, 2009
Last modified: May 27, 2015
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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.