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Q8FYF7

- ODO1_BRUSU

UniProt

Q8FYF7 - ODO1_BRUSU

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Protein

2-oxoglutarate dehydrogenase E1 component

Gene

sucA

Organism
Brucella suis biovar 1 (strain 1330)
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

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:sucAUniRule annotation
Synonyms:odhAUniRule annotation
Ordered Locus Names:BR1923, BS1330_I1917
OrganismiBrucella suis biovar 1 (strain 1330)
Taxonomic identifieri204722 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
ProteomesiUP000000824: Chromosome I, UP000007104: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 100410042-oxoglutarate dehydrogenase E1 componentPRO_0000162171Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi204722.BR1923.

Structurei

3D structure databases

ProteinModelPortaliQ8FYF7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the alpha-ketoglutarate dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0567.
HOGENOMiHOG000259586.
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.

Q8FYF7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAKQEQAPDR ANDVFALTSF LYGGNADYIE ELYAKYEDDP NSVDPQWRDF
60 70 80 90 100
FAKLGDNADD VKKNAEGPSW TRKNWPIAAN GELVSALDGN WAEVEKHVTD
110 120 130 140 150
KLKGKAAKGE AKGAAGTPLT AEEITQAARD SVRAIMMIRA YRMRGHLHAN
160 170 180 190 200
LDPLGLAEKP NDYNELEPEN YGFTPADYNR KIFIDNVLGL EYATVPEMLD
210 220 230 240 250
ILKRTYCGAI GVEFMHISDP AEKAWIQERI EGPDKKVAFT PEGKKAILSK
260 270 280 290 300
LIEAEGFEQF IDVKYKGTKR FGLDGGESLI PALEQIVKRG GQMGLKEVVL
310 320 330 340 350
GMAHRGRLNV LSQVMGKPHR AIFHEFKGGS YTPDDVEGSG DVKYHLGASS
360 370 380 390 400
DREFDGNKVH LSLTANPSHL EIVNPVVMGK ARAKQDLLVG RTRDDMVPLS
410 420 430 440 450
ERAKVLPLLL HGDAAFAGQG VVAECLGLSG LKGHRVAGTL HFIINNQIGF
460 470 480 490 500
TTNPAFSRSS PYPSDVAKMI EAPIFHVNGD DPEAVVFAAK VATEFRMTFH
510 520 530 540 550
KPVVIDMFCY RRFGHNEGDE PSFTQPLMYK AIRAHKTTVQ LYGEKLIAEG
560 570 580 590 600
LVTQDDIDRM KADWRQKLEG EFEAGQSYKP NKADWLDGAW AGLRTADNAD
610 620 630 640 650
EQRRGKTAVP VKTLKEIGKK LVEVPKDFHV HRTIQRFLDN RAKMMETGEG
660 670 680 690 700
IDWATAESLA FGSLAVEGHP IRLSGQDVER GTFSQRHTVL YDQENQNRYI
710 720 730 740 750
PLNNLQKGQA IYEAINSMLS EEAVLGYEYG YSLSDPRALV LWEAQFGDFA
760 770 780 790 800
NGAQVVFDQF ISSGERKWLR MSGLVCLLPH GFEGQGPEHS SARLERYLQL
810 820 830 840 850
CAEDNMQVAN VTTPANYFHI LRRQMKRDFR KPLIMMTPKS LLRHKRAIST
860 870 880 890 900
LAELSGESSF HRLLWDDAQY NKDEGIKLQK DAKIRRVVLC SGKVYYDLYE
910 920 930 940 950
EREKRGIDDV YLLRVEQLYP FPAKALINEL SRFRHAEMVW CQEEPKNMGA
960 970 980 990 1000
WSFIDPYLEW VLAHIDAKHQ RVRYAGRPAA ASPATGLMSK HLAQLAAFLE

DALG
Length:1,004
Mass (Da):112,681
Last modified:March 1, 2003 - v1
Checksum:i390B507D3018DD46
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014291 Genomic DNA. Translation: AAN30815.1.
CP002997 Genomic DNA. Translation: AEM19232.1.
RefSeqiNP_698900.1. NC_004310.3.
YP_005616724.1. NC_017251.1.

Genome annotation databases

EnsemblBacteriaiAAN30815; AAN30815; BR1923.
AEM19232; AEM19232; BS1330_I1917.
GeneIDi1167623.
12137701.
KEGGibms:BR1923.
bsi:BS1330_I1917.
PATRICi17792267. VBIBruSui107850_1958.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014291 Genomic DNA. Translation: AAN30815.1 .
CP002997 Genomic DNA. Translation: AEM19232.1 .
RefSeqi NP_698900.1. NC_004310.3.
YP_005616724.1. NC_017251.1.

3D structure databases

ProteinModelPortali Q8FYF7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 204722.BR1923.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAN30815 ; AAN30815 ; BR1923 .
AEM19232 ; AEM19232 ; BS1330_I1917 .
GeneIDi 1167623.
12137701.
KEGGi bms:BR1923.
bsi:BS1330_I1917.
PATRICi 17792267. VBIBruSui107850_1958.

Phylogenomic databases

eggNOGi COG0567.
HOGENOMi HOG000259586.
KOi K00164.
OMAi GHQNANL.
OrthoDBi EOG6V1M1F.

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: 1330.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 1330.

Entry informationi

Entry nameiODO1_BRUSU
AccessioniPrimary (citable) accession number: Q8FYF7
Secondary accession number(s): G0K866
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: March 1, 2003
Last modified: October 1, 2014
This is version 74 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. Brucella suis
    Brucella suis (strain 1330): entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3