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UniProtKB/Swiss-Prot entry Q7A5N4

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information

Entry name

ODO2_STAAN

Primary accession number

Q7A5N4

Secondary accession numbers

None

Integrated into Swiss-Prot on

May 29, 2007

Sequence was last modified on

July 5, 2004 (Sequence version 1)

Annotations were last modified on

November 25, 2008 (Entry version 35)

Name and origin of the protein

Protein name

Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex

Synonyms

E2
EC 2.3.1.61
Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex

Gene name

	Name:	odhB
	Synonyms:	sucB
	OrderedLocusNames:	SA1244

From

Staphylococcus aureus (strain N315)

[TaxID: 158879]

[HAMAP proteome]

Taxonomy

Bacteria; Firmicutes; Bacillales; Staphylococcus.

Protein existence

1: Evidence at protein level;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1016/S0140-6736(00)04403-2; PubMed=11418146 [NCBI, ExPASy, EBI, Israel, Japan]
Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y., Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K.;
"Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
Lancet 357:1225-1240(2001).

[2]

IDENTIFICATION BY MASS SPECTROMETRY.
Vaezzadeh A.R., Deshusses J., Lescuye P., Hochstrasser D.F.;
"Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315.";
Submitted (OCT-2007) to UniProtKB.

Comments

FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). 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 N⁶-(dihydrolipoyl)lysine = CoA + enzyme N⁶-(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: Forms a 24-polypeptide structural core with octahedral symmetry (By similarity).
SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
SIMILARITY: Contains 1 lipoyl-binding domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BA000018; BAB42504.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

D89918; D89918.

RefSeq

NP_374525.1; -.

3D structure databases

HSSP

P11961; 1B5S. [HSSP ENTRY / PDB]

ModBase

Q7A5N4.

Enzyme and pathway databases

BioCyc

SAUR158879:SA1244-MON; -.

Ontologies

GO:0045252;	Cellular component: oxoglutarate dehydrogenase complex (inferred from electronic annotation from InterPro).
GO:0004149;	Molecular function: dihydrolipoyllysine-residue succinyltransferase activity (inferred from electronic annotation from InterPro).
GO:0031405;	Molecular function: lipoic acid binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005515;	Molecular function: protein binding (inferred from electronic annotation from InterPro).
GO:0006099;	Biological process: tricarboxylic acid cycle (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR003016; 2-oxoA_DHase_lipoyl-BS.
IPR001078; 2Oxoacid_DHase.
IPR000089; Biotin_lipoyl.
IPR004167; E3_bd.
IPR006255; SucB.
Graphical view of domain structure.

Pfam

PF00198; 2-oxoacid_dh; 1.
PF00364; Biotin_lipoyl; 1.
PF02817; E3_binding; 1.
Pfam graphical view of domain structure.

ProDom

PD001115; 2Oxoacid_dh; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR01347; sucB; 1.

PROSITE

PS50968; BIOTINYL_LIPOYL; 1.
PS00189; LIPOYL; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

1124083; -.

GenomeReviews

BA000018_GR; SA1244.

KEGG

sau:SA1244; -.

Phylogenomic databases

HOGENOM

Q7A5N4; -.

Genome annotation databases

CMR

Q7A5N4; SA1244.

Other

ProtoNet

Q7A5N4.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acyltransferase; Complete proteome; Lipoyl; Transferase; Tricarboxylic acid cycle.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 422`	`422`	`Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex.`	`PRO_0000288104`
`DOMAIN`	`2 75`	`74`	`Lipoyl-binding.`
`ACT_SITE`	`393 393`		`By similarity.`
`ACT_SITE`	`397 397`		`By similarity.`
`BINDING`	`42 42`		`Lipoyl (covalent) (Potential).`

Sequence information

Length: 422 AA [This is the length of the unprocessed precursor]

Molecular weight: 46683 Da [This is the MW of the unprocessed precursor]

CRC64: D5A63F50BB766BAB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPEVKVPELA ESITEGTIAE WLKNVGDSVE KGEAILELET DKVNVEVVSE EAGVLSEQLA 

        70         80         90        100        110        120 
SEGDTVEVGQ AIAIIGEGSG NASKENSNDN TPQQNEETNN KKEETTNNSV DKAEVNQAND 

       130        140        150        160        170        180 
DNQQRINATP SARRYARENG VNLAEVSPKT NDVVRKEDID KKQQAPASTQ TTQQAPAKEE 

       190        200        210        220        230        240 
KKYNQYPTKP VIREKMSRRK KTAAKKLLEV SNNTAMLTTF NEVDMTNVME LRKRKKEQFM 

       250        260        270        280        290        300 
KDHDGTKLGF MSFFTKASVA ALKKYPEVNA EIDGDDMITK QYYDIGVAVS TDDGLLVPFV 

       310        320        330        340        350        360 
RDCDKKNFAE IEAEIANLAV KAREKKLGLD DMVNGSFTIT NGGIFGSMMS TPIINGNQAA 

       370        380        390        400        410        420 
ILGMHSIITR PIAIDQDTIE NRPMMYIALS YDHRIIDGKE AVGFLKTIKE LIENPEDLLL 


ES

Q7A5N4 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools