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UniProtKB/Swiss-Prot entry P45119


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

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Entry information
Entry name ODP1_HAEIN
Primary accession number P45119
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    July 22, 2008 (Entry version 57)
Name and origin of the protein
Protein name Pyruvate dehydrogenase E1 component
Synonym EC 1.2.4.1
Gene name
Name: aceE
OrderedLocusNames: HI1233
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: Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.
  • COFACTOR: Thiamine pyrophosphate (By similarity).
  • SUBUNIT: Homodimer (By similarity).
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; AAC22886.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A64112; A64112.
RefSeq NP_439389.1; -.
3D structure databases
HSSP P06958; 1L8A. [HSSP ENTRY / PDB]
ModBase P45119.
Enzyme and pathway databases
BioCyc HINF71421:HI_1233-MON; -.
Ontologies
GO
GO:0004739; Molecular function: pyruvate dehydrogenase (acetyl-transferring) activity (inferred from electronic annotation from EC).
QuickGo view.
Family and domain databases
InterPro IPR004660; 2-oxoA_DHase_E1.
IPR015941; Transketolase_C-like.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.920; Transketo_C_like; 1.
PIRSF PIRSF000156; Pyruvate_dh_E1; 1.
TIGRFAMs TIGR00759; aceE; 1.
BLOCKS P45119.
Genome annotation databases
GeneID 950116; -.
GenomeReviews L42023_GR; HI1233.
KEGG hin:HI1233; -.
NMPDR fig|71421.1.peg.1179; -.
TIGR HI1233; -.
Phylogenomic databases
HOGENOM P45119; -.
Other
ProtoNet P45119.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Glycolysis; Oxidoreductase; Pyruvate; Thiamine pyrophosphate.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
CHAIN   1   886  886     Pyruvate dehydrogenase E1 component. PRO_0000162245
Sequence information
Length: 886 AA [This is the length of the unprocessed precursor] Molecular weight: 99131 Da [This is the MW of the unprocessed precursor] CRC64: 1B936A75DD69E71D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSEILKNDVD PIETQDWLQS LDSLIREEGV ERAQYIVEQV IGQARTSGVS LPTGVTTDYV 

        70         80         90        100        110        120 
NTIPVAEQPA YPGDHAIERR IRSAVRWNAI AMVLRSQKKD LDLGGHISTF QSAATMYEVC 

       130        140        150        160        170        180 
YNHFFKAATE KNGGDLIFFQ GHAAPGMYAR AFLEGRLTEE QMDNFRQEAF TDGLSSYPHP 

       190        200        210        220        230        240 
KLMPEFWQFS TVSMGLGPVN AIYQARFLKY LDNRGLKDTK DQKVYAFLGD GEMDEIESKG 

       250        260        270        280        290        300 
ALTFAAREHL DNLIFTISCN LQRLDGPVNG NGKIVQELEG LFTGAGWEVI KVLWGSDWDK 

       310        320        330        340        350        360 
LFAKDTSGKL TQLMMEVVDG DYLTFKSKDG AYIREHFFGR YPETAALVAD MTDDEIWALR 

       370        380        390        400        410        420 
RGAHDSEKLY AAYAKAQNAT KPVVILAHQV KGYKIPEAES KNTAHQSKKM SYESLKGFRD 

       430        440        450        460        470        480 
FFELPLTDEQ VEKLEYIKFA EGTPEYEYLH GHRKALNGYV PARRTKFDVE YKVPALEEFK 

       490        500        510        520        530        540 
ALLEEQPRGI STTMAFTRAL NILLKDKNIG KTIVPMIADE ARTFGMEGLF RQVGIYNPHG 

       550        560        570        580        590        600 
QNYIPSDRDL VAYYREAKDG QVLQEGINEL GATASWLAAA NSYSVNNQPM IPFFIYYSMF 

       610        620        630        640        650        660 
GFQRVGDMMW AAGDQLARGF MVGGTSGRTT LNGEGLQHED GHSHIQAGII PNCITYDPSF 

       670        680        690        700        710        720 
AFEVAVIMQD GINRMYGEKQ EDVFYYMTTL NEVMDQPAMP AGAEEGIRKG LYKFETVEGK 

       730        740        750        760        770        780 
KGKGHVQLLG SGAIMRHVRE AAQILANDYG VTSDVFSAPS FNELAREGHD AARWNLLHPT 

       790        800        810        820        830        840 
ETQRVPYVAQ VLADLPTVAS TDYVKGYADQ IRAFVPSKHY HVLGTDGFGR SDSRANLREH 

       850        860        870        880 
FEVDARYVVV AALSQLAKEG TVSNQVVADA IAKFGLNVDR INPLYA 

P45119 in FASTA format

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