DP00427: Pyruvate dehydrogenase E1 componentFASTA viewXML view

General information
DisProt:DP00427
Name:Pyruvate dehydrogenase E1 component
Synonym(s):ODP1_ECOLI
EC 1.2.4.1
First appeared in release:Release 3.0 (02/17/2006)
UniProt:P0AFG8
UniGene: 
SwissProt: ODP1_ECOLI
TrEMBL:  
NCBI (GI): 84027826
Source organism:Escherichia coli
Sequence length:887
Percent disordered:10%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MSERFPNDVD PIETRDWLQA IESVIREEGV ERAQYLIDQL LAEARKGGVN VAAGTGISNY - 60
INTIPVEEQP EYPGNLELER RIRSAIRWNA IMTVLRASKK DLELGGHMAS FQSSATIYDV - 120
CFNHFFRARN EQDGGDLVYF QGHISPGVYA RAFLEGRLTQ EQLDNFRQEV HGNGLSSYPH - 180
PKLMPEFWQF PTVSMGLGPI GAIYQAKFLK YLEHRGLKDT SKQTVYAFLG DGEMDEPESK - 240
GAITIATREK LDNLVFVINC NLQRLDGPVT GNGKIINELE GIFEGAGWNV IKVMWGSRWD - 300
ELLRKDTSGK LIQLMNETVD GDYQTFKSKD GAYVREHFFG KYPETAALVA DWTDEQIWAL - 360
NRGGHDPKKI YAAFKKAQET KGKATVILAH TIKGYGMGDA AEGKNIAHQV KKMNMDGVRH - 420
IRDRFNVPVS DADIEKLPYI TFPEGSEEHT YLHAQRQKLH GYLPSRQPNF TEKLELPSLQ - 480
DFGALLEEQS KEISTTIAFV RALNVMLKNK SIKDRLVPII ADEARTFGME GLFRQIGIYS - 540
PNGQQYTPQD REQVAYYKED EKGQILQEGI NELGAGCSWL AAATSYSTNN LPMIPFYIYY - 600
SMFGFQRIGD LCWAAGDQQA RGFLIGGTSG RTTLNGEGLQ HEDGHSHIQS LTIPNCISYD - 660
PAYAYEVAVI MHDGLERMYG EKQENVYYYI TTLNENYHMP AMPEGAEEGI RKGIYKLETI - 720
EGSKGKVQLL GSGSILRHVR EAAEILAKDY GVGSDVYSVT SFTELARDGQ DCERWNMLHP - 780
LETPRVPYIA QVMNDAPAVA STDYMKLFAE QVRTYVPADD YRVLGTDGFG RSDSRENLRH - 840
HFEVDASYVV VAALGELAKR GEIDKKVVAD AIAKFNIDAD KVNPRLA



Functional narrative    

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).

Region 1: 2-56 Region 2: 402-414 Region 3: 542-558

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered
Name: 
Location:2 - 56
Length:55
Region sequence:

SERFPNDVDPIETRDWLQAIESVIREEGVERAQYLIDQLLAEARKGGVNVAAGTG

Modification type: Native
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Cofactor/heme binding
Detection methods:
  1. X-ray crystallography (295 K; Hepes buffer (pH 7.05) 60 mM; NaN3 (0.2%); PEG2000 (15-20%); propanol (10%))

References:
  1. Arjunan P, Nemeria N, Brunskill A, Chandrasekhar K, Sax M, Yan Y, Jordan F, Guest JR, Furey W. "Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution." Biochemistry. 2002; 41(16): 5213-21. PubMed: 11955070

Comments:
 



Region 2
Type:Disordered
Name: 
Location:402 - 414
Length:13
Region sequence:

EGKNIAHQVKKMN

Modification type: Native
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Cofactor/heme binding
Detection methods:
  1. X-ray crystallography (295 K; Hepes buffer (pH 7.05) 60 mM; NaN3 (0.2%); PEG2000 (15-20%); propanol (10%))

References:
  1. Arjunan P, Nemeria N, Brunskill A, Chandrasekhar K, Sax M, Yan Y, Jordan F, Guest JR, Furey W. "Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution." Biochemistry. 2002; 41(16): 5213-21. PubMed: 11955070

Comments:
 



Region 3
Type:Disordered
Name: 
Location:542 - 558
Length:17
Region sequence:

NGQQYTPQDREQVAYYK

Modification type: Native
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Cofactor/heme binding
Detection methods:
  1. X-ray crystallography (295 K; Hepes buffer (pH 7.05) 60 mM; NaN3 (0.2%); PEG2000 (15-20%); propanol (10%))

References:
  1. Arjunan P, Nemeria N, Brunskill A, Chandrasekhar K, Sax M, Yan Y, Jordan F, Guest JR, Furey W. "Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution." Biochemistry. 2002; 41(16): 5213-21. PubMed: 11955070

Comments:
 


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