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Reviewed, UniProtKB/Swiss-Prot P45302 (ODO2_HAEIN)

Last modified June 16, 2009. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
      Short name=E2
    EC=2.3.1.61
Alternative name(s):
    Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex
Gene names
Name: sucB
Ordered Locus Names: HI1661
OrganismHaemophilus influenzae [Complete proteome] [HAMAP]
Taxonomic identifier727 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length409 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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) By similarity.

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 By similarity.

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Contains 1 lipoyl-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 409409Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
PRO_0000162264

Regions

Domain1 – 7676Lipoyl-binding

Sites

Active site3801 Potential
Active site3841 Potential

Amino acid modifications

Modified residue431N6-lipoyllysine Potential

Sequences

Sequence LengthMass (Da)Tools
P45302-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 3FBF62BC17433839

FASTA40945,163
        10         20         30         40         50         60 
MAIEILVPDL PESVADATVA TWHKKLGDTV KRDEVIVEIE TDKVVLEVPA LSDGVLAEVV 

        70         80         90        100        110        120 
QAEGETVVSK QLLGKISTAQ EGDVSSATLK ATNEPTPSDR QNAAIENSHN HNADQSPVIR 

       130        140        150        160        170        180 
RLLAEHDLQA DQIQGSGVGG RLTREDIERE IAKRQAQQVK QEAATEQNTI STVAYSARSE 

       190        200        210        220        230        240 
KRVPMTRLRK RIAERLLEAK NSTAMLTTFN EVDMQPIMTL RKTYGEKFEK QHSVRLGFMS 

       250        260        270        280        290        300 
FYIKAVVEAL KRYPEVNASI DGDDVVYHNY FDISIAVSTP RGLVTPVLRD CDKLSMAEIE 

       310        320        330        340        350        360 
KQIKALAEKG RDGKLTVEDL TGGNFTITNG GVFGSLMSTP IINPPQSAIL GMHAIKERPI 

       370        380        390        400 
ALNGQVVIRP MMYLALSYDH RLIDGRESVG FLVTIKELLE DPTRLLLEI 

« Hide

Cross-references

Sequence databases

L42023 Genomic DNA. Translation: AAC23307.1.
PIRD64135.
RefSeqNP_439803.1.

3D structure databases

HSSPHSSP built from PDB template 1C4T based on UniProtKB P07016.
SMRP45302. Positions 177-409.
ModBaseSearch...

Genome annotation databases

GeneID950492.
GenomeReviewsGene locus HI1661 in contig L42023_GR.
KEGGhin:HI1661.
NMPDRfig|71421.1.peg.1575.
TIGRHI1661.

Phylogenomic databases

HOGENOMP45302.
OMAP45302. LTTYNEV.

Enzyme and pathway databases

BioCycHINF71421:HI_1661-MON.
BRENDA2.3.1.61. 109.

Family and domain databases

InterProIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR004167. E3_bd.
IPR006255. SucB.
[Graphical view]
Gene3DG3DSA:4.10.320.10. E3_bd. 1 hit.
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
ProDomPD001115. 2Oxoacid_dh. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01347. sucB. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameODO2_HAEIN
AccessionPrimary (citable) accession number: P45302
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 16, 2009
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents