P07003 (POXB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pyruvate dehydrogenase [ubiquinone]
EC=1.2.5.1

Alternative name(s):
Pyruvate oxidase
Short name=POX

Cleaved into the following chain:

1. Alpha-peptide

Gene names

Name:	poxB
Ordered Locus Names:	b0871, JW0855

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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

General annotation (Comments)

Catalytic activity	Pyruvate + ubiquinone + H2O = acetate + CO2 + ubiquinol. Ref.9
Cofactor	Binds 1 FAD per subunit. Ref.8 Ref.9 Binds 1 magnesium ion per subunit. Ref.8 Ref.9 Binds 1 thiamine pyrophosphate per subunit. Ref.8 Ref.9
Subunit structure	Homotetramer. Ref.9
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.

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 Reference proteome
Gene Ontology (GO)
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: InterPro pyruvate dehydrogenase (quinone) activity Inferred from electronic annotation. Source: EC thiamine pyrophosphate binding Inferred from electronic annotation. Source: InterPro transferase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 572

572

Pyruvate dehydrogenase [ubiquinone]

PRO_0000044606

Peptide

550 – 572

23

Alpha-peptide

PRO_0000035665

Experimental info

Mutagenesis

533

1

A → T in poxB11.

Mutagenesis

549 – 572

24

Missing in poxB6.

Mutagenesis

553

1

A → V in poxB14.

Mutagenesis

560

1

D → P in poxB15; normal activity.

Mutagenesis

564 – 572

9

Missing in poxB7.

Mutagenesis

564

1

E → P in poxB16; loss of activity.

Mutagenesis

570 – 572

3

Missing in poxB8.

Mutagenesis

572

1

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

Sequence conflict

364 – 365

2

QQ → HE in AAB59101. Ref.5

Sequence conflict

364 – 365

2

QQ → HE in AAB59102. Ref.5

Sequence conflict

414 – 416

3

QAL → HGV in AAB59101. Ref.5

Sequence conflict

414 – 416

3

QAL → HGV in AAB59102. Ref.5

Secondary structure

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572

Helix Strand Turn

Details...

Helix

5 – 15

11

Beta strand

20 – 22

3

Helix

33 – 38

6

Helix

50 – 56

7

Helix

60 – 63

4

Beta strand

68 – 70

3

Helix

79 – 81

3

Helix

86 – 90

5

Beta strand

95 – 100

6

Helix

104 – 106

3

Helix

117 – 120

4

Beta strand

126 – 130

5

Helix

134 – 136

3

Helix

137 – 150

14

Beta strand

155 – 159

5

Helix

163 – 165

3

Beta strand

183 – 185

3

Helix

188 – 199

12

Beta strand

203 – 208

6

Helix

216 – 222

7

Beta strand

230 – 232

3

Turn

238 – 240

3

Beta strand

241 – 243

3

Helix

261 – 265

5

Beta strand

267 – 271

5

Helix

279 – 281

3

Beta strand

284 – 291

8

Helix

295 – 297

3

Beta strand

305 – 308

4

Helix

312 – 319

8

Helix

320 – 322

3

Helix

330 – 343

14

Helix

347 – 349

3

Helix

359 – 369

11

Beta strand

375 – 378

4

Helix

383 – 390

8

Beta strand

398 – 400

3

Helix

411 – 415

5

Turn

419 – 421

3

Beta strand

427 – 431

5

Helix

443 – 448

6

Beta strand

454 – 459

6

Helix

487 – 493

7

Beta strand

499 – 501

3

Helix

504 – 506

3

Helix

507 – 516

10

Beta strand

521 – 527

7

Sequences

	Sequence		Length	Mass (Da)
	P07003 [UniParc]. Last modified April 1, 1988. Version 1. Checksum: 57B38B9E3A92BDEA	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

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. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., 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.
[8]	"Role of the divalent metal cation in the pyruvate oxidase reaction." Blake R. II, O'Brien T.A., Gennis R.B., Hager L.P. J. Biol. Chem. 257:9605-9611(1982) [PubMed: 6286628] [Abstract] Cited for: ENZYME KINETICS, METAL COFACTOR.
[9]	"Reconstitution of native Escherichia coli pyruvate oxidase from apoenzyme monomers and FAD." Recny M.A., Hager L.P. J. Biol. Chem. 257:12878-12886(1982) [PubMed: 6752142] [Abstract] Cited for: CATALYTIC ACTIVITY, SUBUNIT, COFACTOR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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

NP_415392.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P07003.

SMR

P07003. Positions 2-572.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36216N.

IntAct

P07003. 5 interactions.

2D gel databases

SWISS-2DPAGE

P07003.

ECO2DBASE

G058.0. 6TH EDITION.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000000169; EBESCP00000000169; EBESCG00000000136.
EBESCT00000016226; EBESCP00000015517; EBESCG00000015286.

GeneID

946132.

GenomeReviews

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

KEGG

ecj:JW0855.
eco:b0871.

PATRIC

32116949. VBIEscCol129921_0900.

Organism-specific databases

EchoBASE

EB0747.

EcoGene

EG10754. poxB.

Phylogenomic databases

GeneTree

EBGT00050000008285.

OMA

IYGLVGD.

PhylomeDB

P07003.

ProtClustDB

PRK09124.

Enzyme and pathway databases

BioCyc

EcoCyc:PYRUVOXID-MONOMER.
MetaCyc:PYRUVOXID-MONOMER.

Gene expression databases

Genevestigator

P07003.

Family and domain databases

InterPro

IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR000399. TPP-bd_CS.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]

KO

K00156.

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

DrugBank

DB00336. Nitrofurazone.

Entry information

Entry name

POXB_ECOLI

Accession

Primary (citable) accession number: P07003
Secondary accession number(s): Q47513 , Q47514, Q47515, Q47516, Q47517, Q47518, Q47519, Q47520

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	April 1, 1988
Last modified:	January 25, 2012
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program