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UniProtKB/Swiss-Prot entry P45302

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

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Entry information

Entry name

ODO2_HAEIN

Primary accession number

P45302

Secondary accession numbers

None

Integrated into Swiss-Prot on

November 1, 1995

Sequence was last modified on

November 1, 1995 (Sequence version 1)

Annotations were last modified on

November 25, 2008 (Entry version 68)

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:	sucB
	OrderedLocusNames:	HI1661

From

Haemophilus influenzae

[TaxID: 727]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; Pasteurellaceae; Haemophilus.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
PubMed=7542800 [NCBI, ExPASy, EBI, Israel, Japan]
Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd.";
Science 269:496-512(1995).

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

L42023; AAC23307.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

D64135; D64135.

RefSeq

NP_439803.1; -.

3D structure databases

HSSP

P07016; 1C4T. [HSSP ENTRY / SWISS-3DIMAGE / PDB]

SMR

P45302; 177-409.

ModBase

P45302.

Enzyme and pathway databases

BioCyc

HINF71421:HI_1661-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).

Genome annotation databases

950492; -.

L42023_GR; HI1661.

hin:HI1661; -.

fig|71421.1.peg.1575; -.

TIGR

HI1661; -.

Phylogenomic databases

HOGENOM

P45302; -.

Other

ProtoNet

P45302.

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`	`1 409`	`409`	`Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex.`	`PRO_0000162264`
`DOMAIN`	`1 76`	`76`	`Lipoyl-binding.`
`ACT_SITE`	`380 380`		`Potential.`
`ACT_SITE`	`384 384`		`Potential.`
`BINDING`	`43 43`		`Lipoyl (covalent) (Potential).`

Sequence information

Length: 409 AA [This is the length of the unprocessed precursor]

Molecular weight: 45163 Da [This is the MW of the unprocessed precursor]

CRC64: 3FBF62BC17433839 [This is a checksum on the sequence]

        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

P45302 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