Pyruvate dehydrogenase [cytochrome] - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P07003 (POXB_ECOLI)

Last modified June 16, 2009. Version 92. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Pyruvate dehydrogenase [cytochrome]
    EC=1.2.2.2
Alternative name(s):
    Pyruvate oxidase
      Short name=POX
    Pyruvate dehydrogenase [Ubiquinone]
Cleaved into the following chain:
    1- Recommended name:
            Alpha-peptide

Gene names

Name:	poxB
Ordered Locus Names:	b0871, JW0855

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	572 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	Pyruvate + ferricytochrome b1 + H₂O = acetate + CO₂ + ferrocytochrome b1.
Cofactor	Binds 1 FAD per subunit. Binds 1 magnesium ion per subunit. Binds 1 thiamine pyrophosphate per subunit.
Subunit structure	Homotetramer.
Subcellular location	Cell membrane; Peripheral membrane protein.
Post-translational modification	Activated by limited proteolytic digestion. This cleavage produces a peptide (alpha-peptide) and mimics the activation of enzyme by phospholipids. The proteolytic cleavage also results in the loss of the high affinity lipid-binding site of the enzyme.
Sequence similarities	Belongs to the TPP enzyme family.

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Ontologies

Keywords
Cellular component	Cell membrane Membrane
Ligand	FAD Flavoprotein Lipid-binding Magnesium Thiamine pyrophosphate
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	lipid binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct pyruvate dehydrogenase (cytochrome) activity Inferred from electronic annotation. Source: EC thiamin pyrophosphate binding Inferred from electronic annotation. Source: InterPro transferase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
hcp	P75825	1	EBI-909338,EBI-561591

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 572

572

Pyruvate dehydrogenase [cytochrome]

PRO_0000044606

Peptide

550 – 572

Alpha-peptide

PRO_0000035665

Experimental info

Mutagenesis

533

A → T in poxB11.

Mutagenesis

549 – 572

Missing in poxB6.

Mutagenesis

553

A → V in poxB14.

Mutagenesis

560

D → P in poxB15; normal activity.

Mutagenesis

564 – 572

Missing in poxB7.

Mutagenesis

564

E → P in poxB16; loss of activity.

Mutagenesis

570 – 572

Missing in poxB8.

Mutagenesis

572

R → G in poxB10; reduced activity; may interact less with membranes.

Sequence conflict

364 – 365

QQ → HE in AAB59101. Ref.5

Sequence conflict

364 – 365

QQ → HE in AAB59102. Ref.5

Sequence conflict

414 – 416

QAL → HGV in AAB59101. Ref.5

Sequence conflict

414 – 416

QAL → HGV in AAB59102. Ref.5

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Sequences

Sequence

Length

Mass (Da)

Tools

P07003-1 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: 57B38B9E3A92BDEA
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FASTA

572

62,011

        10         20         30         40         50         60 
MKQTVAAYIA KTLESAGVKR IWGVTGDSLN GLSDSLNRMG TIEWMSTRHE EVAAFAAGAE 

        70         80         90        100        110        120 
AQLSGELAVC AGSCGPGNLH LINGLFDCHR NHVPVLAIAA HIPSSEIGSG YFQETHPQEL 

       130        140        150        160        170        180 
FRECSHYCEL VSSPEQIPQV LAIAMRKAVL NRGVSVVVLP GDVALKPAPE GATMHWYHAP 

       190        200        210        220        230        240 
QPVVTPEEEE LRKLAQLLRY SSNIALMCGS GCAGAHKELV EFAGKIKAPI VHALRGKEHV 

       250        260        270        280        290        300 
EYDNPYDVGM TGLIGFSSGF HTMMNADTLV LLGTQFPYRA FYPTDAKIIQ IDINPASIGA 

       310        320        330        340        350        360 
HSKVDMALVG DIKSTLRALL PLVEEKADRK FLDKALEDYR DARKGLDDLA KPSEKAIHPQ 

       370        380        390        400        410        420 
YLAQQISHFA ADDAIFTCDV GTPTVWAARY LKMNGKRRLL GSFNHGSMAN AMPQALGAQA 

       430        440        450        460        470        480 
TEPERQVVAM CGDGGFSMLM GDFLSVVQMK LPVKIVVFNN SVLGFVAMEM KAGGYLTDGT 

       490        500        510        520        530        540 
ELHDTNFARI AEACGITGIR VEKASEVDEA LQRAFSIDGP VLVDVVVAKE ELAIPPQIKL 

       550        560        570 
EQAKGFSLYM LRAIISGRGD EVIELAKTNW LR

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence and deduced amino acid sequence of Escherichia coli pyruvate oxidase, a lipid-activated flavoprotein." Grabau C., Cronan J.E. Jr. Nucleic Acids Res. 14:5449-5460(1986) [PubMed: 3016647] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: K12.
[2]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Lipid binding by Escherichia coli pyruvate oxidase is disrupted by small alterations of the carboxyl-terminal region." Grabau C., Chang Y.Y., Cronan J.E. Jr. J. Biol. Chem. 264:12510-12519(1989) [PubMed: 2663858] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS. Strain: K12.
[6]	"Characterization of the alpha-peptide released upon protease activation of pyruvate oxidase." Recny M.A., Grabau C., Cronan J.E. Jr., Hager L.P. J. Biol. Chem. 260:14287-14291(1985) [PubMed: 3902830] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 550-572.
[7]	"Expression of Escherichia coli pyruvate oxidase (PoxB) depends on the sigma factor encoded by the rpoS(katF) gene." Chang Y.Y., Wang A.Y., Cronan J.E. Jr. Mol. Microbiol. 11:1019-1028(1994) [PubMed: 8022274] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

X04105 Genomic DNA. Translation: CAA27725.1.
U00096 Genomic DNA. Translation: AAC73958.1.
AP009048 Genomic DNA. Translation: BAA35585.1.
S73268 Genomic DNA. Translation: AAB31180.1.
M28208 Genomic DNA. Translation: AAB59101.1.
L47688 Genomic DNA. Translation: AAB59102.1.
L47689 Genomic DNA. Translation: AAB59103.1.
L47690 Genomic DNA. Translation: AAB59104.1.
L47691 Genomic DNA. Translation: AAB59105.1.
L47692 Genomic DNA. Translation: AAB59106.1.
L47693 Genomic DNA. Translation: AAB59107.1.
L47694 Genomic DNA. Translation: AAB59108.1.
L47695 Genomic DNA. Translation: AAB59109.1.

PIR

DEECPC. A23648.

RefSeq

AP_001502.1.
NP_415392.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3EY9	X-ray	2.90	A/B	1-572	[»]
3EYA	X-ray	2.50	A/B/C/D/E/F/G/H/I/J/K/L	1-549	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P07003. 3 interactions.

2-D gel databases

SWISS-2DPAGE

P07003.

ECO2DBASE

G058.0. 6TH EDITION.

Genome annotation databases

GeneID

946132.

GenomeReviews

Gene locus JW0855 in contig AP009048_GR.
Gene locus b0871 in contig U00096_GR.

KEGG

ecj:JW0855.
eco:b0871.

Organism-specific databases

EchoBASE

EB0747.

EcoGene

EG10754. poxB.

CMR

Search...

Phylogenomic databases

OMA

P07003. KTDRKFL.

Enzyme and pathway databases

BioCyc

EcoCyc:PYRUVOXID-MON.
MetaCyc:PYRUVOXID-MON.

Family and domain databases

InterPro

IPR000399. TPP_bd_CS.
IPR012001. TPP_bd_enzyme_N.
IPR011766. TPP_enzyme_bd_C.
IPR012000. TPP_enzyme_M.
[Graphical view]

Pfam

PF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]

PROSITE

PS00187. TPP_ENZYMES. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00336. Nitrofurazone.

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Entry information

Entry name

POXB_ECOLI

Accession

Primary (citable) accession number: P07003
Secondary accession number(s): Q47513

Q47520

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	April 1, 1988
Last modified:	June 16, 2009
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2-D gel databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other Resources

Entry information

Relevant documents