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Protein

Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex

Gene

sucB

Organism
Rickettsia prowazekii (strain Madrid E)
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) (By similarity).By similarity

Catalytic activityi

Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine.

Cofactori

(R)-lipoateBy similarityNote: Binds 1 lipoyl cofactor covalently.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei372 – 3721Sequence Analysis
Active sitei376 – 3761Sequence Analysis

GO - Molecular functioni

  1. dihydrolipoyllysine-residue succinyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. L-lysine catabolic process to acetyl-CoA via saccharopine Source: UniProtKB-UniPathway
  2. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

UniPathwayiUPA00868; UER00840.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (EC:2.3.1.61)
Alternative name(s):
2-oxoglutarate dehydrogenase complex component E2
Short name:
OGDC-E2
Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex
Gene namesi
Name:sucB
Ordered Locus Names:RP179
OrganismiRickettsia prowazekii (strain Madrid E)
Taxonomic identifieri272947 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group
ProteomesiUP000002480: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. oxoglutarate dehydrogenase complex Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 401401Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complexPRO_0000162269Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431N6-lipoyllysinePROSITE-ProRule annotation

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry.By similarity

Protein-protein interaction databases

STRINGi272947.RP179.

Structurei

3D structure databases

ProteinModelPortaliQ9ZDY4.
SMRiQ9ZDY4. Positions 174-398.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 7776Lipoyl-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 1 lipoyl-binding domain.CuratedPROSITE-ProRule annotation

Keywords - Domaini

Lipoyl

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281563.
KOiK00658.
OMAiIETDKVM.
OrthoDBiEOG610413.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
IPR006255. SucB.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR01347. sucB. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9ZDY4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVKIIIPSL GESVTEATIA KWYKKLGDSV KTDELLLEIE TEKVTLEVNA
60 70 80 90 100
PCNGTIEKIA KTDGANVTVG EEIGEINEVV DTDTACTNNN SYKKQAIVQH
110 120 130 140 150
DSEQIVDKPA SSSNILAPSV QKLVTENKLD PNNIKGTGRG GRITKCDVLE
160 170 180 190 200
TINTTPVTIE TPALNKTNEE RTQRVRMSRL RKTIAQRLKD SQNTAAILTT
210 220 230 240 250
FNEIDMSKVI ALRNQYKEEF EKKHTVKLGF MSFFVKATIE ALKLIPSINA
260 270 280 290 300
EIDGDDLLYK NYYDIGVAVG TDQGLVVPVV RDADKMGFAD VEQAIGDLAK
310 320 330 340 350
KAREGKLSMS DLSGGTFSIS NGGVYGSLLS TPIINPPQSG ILGLHKTEER
360 370 380 390 400
AVVIDGKIEI RPMMYIALSY DHRIIDGKEG VSFLVKIKNL IENPEKLLLN

L
Length:401
Mass (Da):43,979
Last modified:May 1, 1999 - v1
Checksum:i353F81339C5E9F23
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ235270 Genomic DNA. Translation: CAA14646.1.
PIRiG71728.
RefSeqiNP_220569.1. NC_000963.1.

Genome annotation databases

EnsemblBacteriaiCAA14646; CAA14646; CAA14646.
GeneIDi883874.
KEGGirpr:RP179.
PATRICi17901108. VBIRicPro72556_0184.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ235270 Genomic DNA. Translation: CAA14646.1.
PIRiG71728.
RefSeqiNP_220569.1. NC_000963.1.

3D structure databases

ProteinModelPortaliQ9ZDY4.
SMRiQ9ZDY4. Positions 174-398.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272947.RP179.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAA14646; CAA14646; CAA14646.
GeneIDi883874.
KEGGirpr:RP179.
PATRICi17901108. VBIRicPro72556_0184.

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281563.
KOiK00658.
OMAiIETDKVM.
OrthoDBiEOG610413.

Enzyme and pathway databases

UniPathwayiUPA00868; UER00840.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
IPR006255. SucB.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR01347. sucB. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Madrid E.

Entry informationi

Entry nameiODO2_RICPR
AccessioniPrimary (citable) accession number: Q9ZDY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: January 7, 2015
This is version 98 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, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Rickettsia prowazekii
    Rickettsia prowazekii (strain Madrid E): entries and gene names
  3. 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.