Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P52993 (ODO2_CUPNH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:sucB
Synonyms:odhB
Ordered Locus Names:H16_A2324
OrganismCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha) [Complete proteome] [HAMAP]
Taxonomic identifier381666 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length416 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 activity

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

Cofactor

Binds 1 lipoyl cofactor covalently By similarity.

Pathway

Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.

Subunit structure

Forms a 24-polypeptide structural core with octahedral symmetry.

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Contains 1 lipoyl-binding domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 416416Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
PRO_0000162253

Regions

Domain1 – 7777Lipoyl-binding

Sites

Active site3871 By similarity
Active site3911 By similarity

Amino acid modifications

Modified residue441N6-lipoyllysine Potential

Sequences

Sequence LengthMass (Da)Tools
P52993 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 100D839352D0A8DF

FASTA41643,250
        10         20         30         40         50         60 
MAIVDVKVPQ LSESVAEATM LNWKKKPGEA VAQDEILIEI ETDKVVLEVP APSAGVLSII 

        70         80         90        100        110        120 
VKNDGDTVVA DEIIAKIDTE ATAGAAAPAA AAPAPAAAAP APAAAVAAPA AAGGVAMPSA 

       130        140        150        160        170        180 
AKLMAEAGLS AGQVAGTGKD GRITKGDALA AAAAPAAKAA PAPAAAKPAL QQVSAPVDFA 

       190        200        210        220        230        240 
ALGDRPEERV PMSRLRARIA ERLLQSQSTN AILTTFNEVN MKPVMDLRNK YKDRFEKEHG 

       250        260        270        280        290        300 
VKLGFMSFFV KAAVHALKKF PLINASIDGN DIVYHGYFDI GIAVGSPRGL VVPILRNADQ 

       310        320        330        340        350        360 
MSLADIEKKI AEFGVKARDG KLSLEELTGG TFSISNGGVF GSMLSTPIIN PPQSAILGVH 

       370        380        390        400        410 
ATKDRPVVED GQIVIRPMNY LAMSYDHRII DGREAVLGLV AMKDALEDPA RLLLDL 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of the Alcaligenes eutrophus 2-oxoglutarate dehydrogenase complex."
Hein S., Steinbuechel A.
FEMS Microbiol. Lett. 136:231-238(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16."
Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.
Nat. Biotechnol. 24:1257-1262(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X91877 Genomic DNA. Translation: CAA62981.1.
AM260479 Genomic DNA. Translation: CAJ93420.1.
PIRT44423.
RefSeqYP_726788.1. NC_008313.1.

3D structure databases

ProteinModelPortalP52993.
SMRP52993. Positions 185-416.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING381666.H16_A2324.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ93420; CAJ93420; H16_A2324.
GeneID4249724.
KEGGreh:H16_A2324.
PATRIC35234167. VBIRalEut6770_2730.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000281563.
KOK00658.
OMAVRTYADQ.
OrthoDBEOG610413.

Enzyme and pathway databases

BioCycCNEC381666:GJUJ-2292-MONOMER.
UniPathwayUPA00868; UER00840.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProIPR003016. 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]
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsTIGR01347. sucB. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameODO2_CUPNH
AccessionPrimary (citable) accession number: P52993
Secondary accession number(s): Q0K9A1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways