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

Q49XM4 (ODO2_STAS1) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 66. 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:odhB
Synonyms:sucB
Ordered Locus Names:SSP1326
OrganismStaphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229) [Complete proteome] [HAMAP]
Taxonomic identifier342451 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length424 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) 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.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 424424Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
PRO_0000288110

Regions

Domain2 – 7574Lipoyl-binding

Sites

Active site3951 By similarity
Active site3991 By similarity

Amino acid modifications

Modified residue421N6-lipoyllysine Potential

Sequences

Sequence LengthMass (Da)Tools
Q49XM4 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 22C7B00CAFECFACE

FASTA42446,457
        10         20         30         40         50         60 
MPEVKVPELA ESITEGTIAE WLKQVGDSVD KGEAIVELET DKVNVEVVSE EAGVLQELLA 

        70         80         90        100        110        120 
NEGDTVEVGQ AIAVVGEGSG NNTSEAPAKQ EAPKQETETS TDDKSAQPAE ATSNDTDDKS 

       130        140        150        160        170        180 
QDNNQRVNAT PSARKYAREK GIDLSEIAAA SNDVVRKEHV DQSQTQTSTQ QQAQPAAKEE 

       190        200        210        220        230        240 
TKKLTQQNPS KPVIREKMSR RKKTAAKKLL EVSNNTAMLT TFNEIDMTNV MDLRKRKKEQ 

       250        260        270        280        290        300 
FIKDHDGTKL GFMSFFTKAA VAALKKYPEV NAEIDGDDMI TKQYYDIGVA VSTEDGLLVP 

       310        320        330        340        350        360 
FVRDCDKKNF AEIEDEIGNL AKKARDKKLG LDDMVNGSFT ITNGGIFGSM MSTPIINGSQ 

       370        380        390        400        410        420 
AAILGMHSII TRPIAIDADT IENRPMMYIA LSYDHRIIDG KEAVGFLKTI KELIENPEDL 


LLES 

« Hide

References

[1]"Whole genome sequence of Staphylococcus saprophyticus reveals the pathogenesis of uncomplicated urinary tract infection."
Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.
Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15305 / DSM 20229.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008934 Genomic DNA. Translation: BAE18471.1.
RefSeqYP_301416.1. NC_007350.1.

3D structure databases

ProteinModelPortalQ49XM4.
SMRQ49XM4. Positions 195-421.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING342451.SSP1326.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE18471; BAE18471; SSP1326.
GeneID3616664.
KEGGssp:SSP1326.
PATRIC19624244. VBIStaSap90642_1329.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000281563.
KOK00658.
OMAQEDETVE.
OrthoDBEOG610413.
ProtClustDBPRK05704.

Enzyme and pathway databases

BioCycSSAP342451:GKFA-1385-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]
SUPFAMSSF51230. SSF51230. 1 hit.
TIGRFAMsTIGR01347. sucB. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameODO2_STAS1
AccessionPrimary (citable) accession number: Q49XM4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: September 13, 2005
Last modified: November 13, 2013
This is version 66 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