NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC VR-358 / Fuller / CIP 107027;
DOI=10.1128/IAI.71.8.4818-4822.2003; PubMed=12874367 [NCBI, ExPASy, EBI, Israel, Japan]
Gilmore R.D. Jr., Carpio A.M., Kosoy M.Y., Gage K.L.;
"Molecular characterization of the sucB gene encoding the immunogenic dihydrolipoamide succinyltransferase protein of Bartonella vinsonii subsp. berkhoffii and Bartonella quintana.";
Infect. Immun. 71:4818-4822(2003).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Toulouse;
DOI=10.1073/pnas.0305659101; PubMed=15210978 [NCBI, ExPASy, EBI, Israel, Japan]
Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E.;
"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae.";
Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).

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 3 enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).
CATALYTIC ACTIVITY: Succinyl-CoA + enzyme N⁶-(dihydrolipoyl)lysine = CoA + enzyme N⁶-(S-succinyldihydrolipoyl)lysine.
COFACTOR: Binds 1 lipoyl cofactor covalently.
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

AY160680; AAN78229.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BX897700; CAF26799.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_032855.1; -.

3D structure databases

HSSP

P07016; 1E2O. [HSSP ENTRY / SWISS-3DIMAGE / PDB]

ModBase

Q6FYD4.

Enzyme and pathway databases

BioCyc

BQUI283165:BQ13410-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.

Gene3D

G3DSA:4.10.320.10; E3_bd; 1.

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).

ProtoNet

Q6FYD4.

Genome annotation databases

GeneID

2866355; -.

GenomeReviews

BX897700_GR; BQ13410.

KEGG

bqu:BQ13410; -.

NMPDR

fig|283165.1.peg.1125; -.

Phylogenomic databases

HOGENOM

Q6FYD4; -.

Genome annotation databases

CMR

Q6FYD4; BQ13410.

Other

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`	`1 410`	`410`	`Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex.`	`PRO_0000162257`
`DOMAIN`	`2 76`	`75`	`Lipoyl-binding.`
`ACT_SITE`	`381 381`		`By similarity.`
`ACT_SITE`	`385 385`		`By similarity.`
`BINDING`	`43 43`		`Lipoyl (covalent) (Potential).`
`CONFLICT`	`4 4`		`G -> E (in Ref. 1; AAN78229).`

Sequence information

Length: 410 AA [This is the length of the unprocessed precursor]

Molecular weight: 43763 Da [This is the MW of the unprocessed precursor]

CRC64: 216936AE2432DC05 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTTGIRVPTL GESVTEATIG KWFKKLGEAV AVDEPLVELE TDKVTVEVPS PVMGKLTEII 

        70         80         90        100        110        120 
AKEGDIVEVN AVLGFVESGA AGISQSFSPS ATSIPEAPSE LEQSPSSSAT PSGTMPPAPS 

       130        140        150        160        170        180 
AAKLMAENNI AKSDISGSGK RGQILKEDVL GALAQGTKAS TSVATLTASS SSAAPIQEMR 

       190        200        210        220        230        240 
EERVRMTKLR QTIARRLKDA QNTAAMLTTF NEVDMSAVMD LRKRYKDLFE KKHGVKLGFM 

       250        260        270        280        290        300 
GFFTKAVCHA LKEFPTVNAE IDGTDIVYKN YVNAGIAVGT DKGLVVPVVR DADQMSLAEI 

       310        320        330        340        350        360 
EKEISRLGRL ARDGKLAVSD MQGGTFTITN GGVYGSLMST PILNAPQSGI LGMHAIKERA 

       370        380        390        400        410 
MVVGGQIIIC PMMYLALSYD HRIVDGQEAV TFLVRVKESL EDPERLVLDL

Q6FYD4 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