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UniProtKB/Swiss-Prot entry P45118

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

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Entry information

Entry name

ODP2_HAEIN

Primary accession number

P45118

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 66)

Name and origin of the protein

Protein name

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Synonyms

EC 2.3.1.12
E2
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex

Gene name

	Name:	aceF
	OrderedLocusNames:	HI1232

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 pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
CATALYTIC ACTIVITY: Acetyl-CoA + enzyme N⁶-(dihydrolipoyl)lysine = CoA + enzyme N⁶-(S-acetyldihydrolipoyl)lysine.
COFACTOR: Binds 2 lipoyl cofactors covalently (By similarity).
SUBUNIT: Forms a 24-polypeptide structural core with octahedral symmetry (By similarity).
SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
SIMILARITY: Contains 2 lipoyl-binding domains.

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; AAC22885.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

I64111; I64111.

RefSeq

NP_439388.1; -.

3D structure databases

HSSP

P06959; 1QJO. [HSSP ENTRY / PDB]

SMR

P45118; 108-186.

ModBase

P45118.

Enzyme and pathway databases

BioCyc

HINF71421:HI_1232-MON; -.

Ontologies

GO:0045254;	Cellular component: pyruvate dehydrogenase complex (inferred from electronic annotation from InterPro).
GO:0004742;	Molecular function: dihydrolipoyllysine-residue acetyltransferase 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:0006096;	Biological process: glycolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR003016; 2-oxoA_DHase_lipoyl-BS.
IPR001078; 2Oxoacid_DHase.
IPR006256; AcTrfase_Pyrv_DHase_cplx.
IPR000089; Biotin_lipoyl.
IPR004167; E3_bd.
Graphical view of domain structure.

Gene3D

G3DSA:4.10.320.10; E3_bd; 1.

Pfam

PF00198; 2-oxoacid_dh; 1.
PF00364; Biotin_lipoyl; 2.
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

TIGR01348; PDHac_trf_long; 1.

PROSITE

PS50968; BIOTINYL_LIPOYL; 2.
PS00189; LIPOYL; 2.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P45118.

Genome annotation databases

949836; -.

L42023_GR; HI1232.

hin:HI1232; -.

fig|71421.1.peg.1178; -.

TIGR

HI1232; -.

Phylogenomic databases

HOGENOM

P45118; -.

Other

UniRef

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

Keywords

Acyltransferase; Complete proteome; Glycolysis; Lipoyl; Repeat; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 567`	`567`	`Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex.`	`PRO_0000162279`
`DOMAIN`	`1 74`	`74`	`Lipoyl-binding 1.`
`DOMAIN`	`109 180`	`72`	`Lipoyl-binding 2.`
`REGION`	`247 567`	`321`	`Subunit binding, catalytic.`
`ACT_SITE`	`484 484`		`Potential.`
`ACT_SITE`	`540 540`		`Potential.`
`ACT_SITE`	`544 544`		`Potential.`
`BINDING`	`41 41`		`Lipoyl (covalent) (By similarity).`
`BINDING`	`147 147`		`Lipoyl (covalent) (By similarity).`

Sequence information

Length: 567 AA [This is the length of the unprocessed precursor]

Molecular weight: 59411 Da [This is the MW of the unprocessed precursor]

CRC64: 891DBCDEB388C5B0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSKQIQIPDI GSDEVTVTEV MVNVGDTISV DQSIINVEGD KASMEVPAPE AGVVKEILVK 

        70         80         90        100        110        120 
VGDKVSTGTP MLVLEAAGAA PAADEPTAPV ADAPTAPVVA TAPTASAIVE VNVPDIGGDE 

       130        140        150        160        170        180 
VNVTEIMVAV GDTITEEQSL ITVEGDKASM EVPAPFGGVV KEILVKSGDK VSTGSLIMRF 

       190        200        210        220        230        240 
EVLGAAPAES ASAPASTSAP QTAAPATTAQ APQAAAPDTT AQAPQAAAPD TTAQAAQSNN 

       250        260        270        280        290        300 
NVSGLSQEQV EASTGYAHAT PVIRRLAREF GVNLDKVKGT GRKGRIVKED IEAYVKTAVK 

       310        320        330        340        350        360 
AYESGATAQA TGNGVANGAG LGLLPWPKVD FSKFGEIEEV ELSRINKISG ANLHRNWVII 

       370        380        390        400        410        420 
PHVTHFDKAD ITDLEAFRKE QNALREKQKL GVKITPVVFI MKAVAKALEA YPRFNSSITE 

       430        440        450        460        470        480 
DAQRLILKKY INIGVAVDTP NGLVVPVFKN VNKKGIIELS RELMEVSKKA REGKLTASDM 

       490        500        510        520        530        540 
QGGCFTISSL GGIGTTHFAP IVNAPEVAIL GVSKSSMEPV WNGKEFAPRL ILPMSLSFDH 

       550        560 
RVIDGADGAR FISYLGSVLA DLRRLVM

P45118 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