| 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
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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
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| 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).
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| 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.
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| 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:
- X-ray crystallography (295 K; Hepes buffer (pH 7.05) 60 mM; NaN3 (0.2%); PEG2000 (15-20%); propanol (10%))
| References:
- 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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| 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:
- X-ray crystallography (295 K; Hepes buffer (pH 7.05) 60 mM; NaN3 (0.2%); PEG2000 (15-20%); propanol (10%))
| References:
- 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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| 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:
- X-ray crystallography (295 K; Hepes buffer (pH 7.05) 60 mM; NaN3 (0.2%); PEG2000 (15-20%); propanol (10%))
| References:
- 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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