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Protein

Pyruvate dehydrogenase [ubiquinone]

Gene

poxB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalytic activityi

Pyruvate + ubiquinone + H2O = acetate + CO2 + ubiquinol.1 Publication

Cofactori

Protein has several cofactor binding sites:
  • FAD1 PublicationNote: Binds 1 FAD per subunit.1 Publication
  • Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication
  • thiamine diphosphate1 PublicationNote: Binds 1 thiamine pyrophosphate per subunit.1 Publication

GO - Molecular functioni

  • flavin adenine dinucleotide binding Source: EcoCyc
  • identical protein binding Source: EcoCyc
  • lipid binding Source: EcoCyc
  • magnesium ion binding Source: EcoCyc
  • pyruvate dehydrogenase (quinone) activity Source: EcoCyc
  • thiamine pyrophosphate binding Source: EcoCyc

GO - Biological processi

  • protein homotetramerization Source: EcoCyc
  • pyruvate catabolic process Source: EcoCyc
  • pyruvate metabolic process Source: EcoCyc

Keywordsi

Molecular functionOxidoreductase
LigandFAD, Flavoprotein, Lipid-binding, Magnesium, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciEcoCyc:PYRUVOXID-MONOMER
MetaCyc:PYRUVOXID-MONOMER
BRENDAi1.2.5.1 2026

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase [ubiquinone] (EC:1.2.5.1)
Alternative name(s):
Pyruvate oxidase
Short name:
POX
Cleaved into the following chain:
Gene namesi
Name:poxB
Ordered Locus Names:b0871, JW0855
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10754 poxB

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • plasma membrane Source: UniProtKB-SubCell

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi533A → T in poxB11. 1 Publication1
Mutagenesisi549 – 572Missing in poxB6. 1 PublicationAdd BLAST24
Mutagenesisi553A → V in poxB14. 1 Publication1
Mutagenesisi560D → P in poxB15; normal activity. 1 Publication1
Mutagenesisi564 – 572Missing in poxB7. 1 Publication9
Mutagenesisi564E → P in poxB16; loss of activity. 1 Publication1
Mutagenesisi570 – 572Missing in poxB8. 1 Publication3
Mutagenesisi572R → G in poxB10; reduced activity; may interact less with membranes. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL3380
DrugBankiDB00336 Nitrofural

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000446061 – 572Pyruvate dehydrogenase [ubiquinone]Add BLAST572
PeptideiPRO_0000035665550 – 572Alpha-peptideAdd BLAST23

Post-translational modificationi

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.

Proteomic databases

EPDiP07003
PaxDbiP07003
PRIDEiP07003

2D gel databases

SWISS-2DPAGEiP07003

Interactioni

Subunit structurei

Homotetramer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-909338,EBI-909338

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4262101, 20 interactors
DIPiDIP-36216N
IntActiP07003, 4 interactors
STRINGi316385.ECDH10B_0941

Structurei

Secondary structure

1572
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 15Combined sources11
Beta strandi20 – 23Combined sources4
Helixi27 – 29Combined sources3
Helixi30 – 39Combined sources10
Beta strandi41 – 46Combined sources6
Helixi50 – 64Combined sources15
Beta strandi68 – 72Combined sources5
Helixi76 – 79Combined sources4
Helixi82 – 90Combined sources9
Beta strandi95 – 102Combined sources8
Helixi104 – 106Combined sources3
Helixi117 – 120Combined sources4
Turni121 – 124Combined sources4
Beta strandi126 – 130Combined sources5
Helixi134 – 136Combined sources3
Helixi137 – 150Combined sources14
Beta strandi153 – 160Combined sources8
Helixi161 – 164Combined sources4
Beta strandi183 – 185Combined sources3
Helixi188 – 199Combined sources12
Beta strandi203 – 208Combined sources6
Helixi210 – 212Combined sources3
Helixi216 – 226Combined sources11
Beta strandi230 – 232Combined sources3
Helixi234 – 236Combined sources3
Helixi237 – 240Combined sources4
Beta strandi241 – 243Combined sources3
Beta strandi247 – 250Combined sources4
Helixi257 – 265Combined sources9
Beta strandi267 – 273Combined sources7
Helixi279 – 281Combined sources3
Beta strandi284 – 293Combined sources10
Helixi295 – 297Combined sources3
Beta strandi300 – 302Combined sources3
Beta strandi305 – 309Combined sources5
Helixi312 – 319Combined sources8
Helixi320 – 322Combined sources3
Helixi330 – 348Combined sources19
Beta strandi349 – 351Combined sources3
Beta strandi354 – 357Combined sources4
Helixi359 – 369Combined sources11
Beta strandi375 – 378Combined sources4
Helixi382 – 390Combined sources9
Beta strandi398 – 400Combined sources3
Turni403 – 405Combined sources3
Helixi411 – 421Combined sources11
Beta strandi427 – 432Combined sources6
Helixi433 – 438Combined sources6
Helixi440 – 442Combined sources3
Helixi443 – 448Combined sources6
Beta strandi454 – 459Combined sources6
Beta strandi461 – 466Combined sources6
Beta strandi468 – 470Combined sources3
Turni478 – 480Combined sources3
Helixi487 – 493Combined sources7
Beta strandi496 – 501Combined sources6
Helixi504 – 506Combined sources3
Helixi507 – 516Combined sources10
Beta strandi517 – 519Combined sources3
Beta strandi521 – 527Combined sources7
Helixi536 – 542Combined sources7
Turni543 – 545Combined sources3
Helixi548 – 550Combined sources3
Beta strandi551 – 555Combined sources5
Beta strandi559 – 564Combined sources6

3D structure databases

ProteinModelPortaliP07003
SMRiP07003
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07003

Family & Domainsi

Sequence similaritiesi

Belongs to the TPP enzyme family.Curated

Phylogenomic databases

eggNOGiENOG4105C7K Bacteria
COG0028 LUCA
InParanoidiP07003
KOiK00156
OMAiRGKEWIQ
PhylomeDBiP07003

Family and domain databases

InterProiView protein in InterPro
IPR029035 DHS-like_NAD/FAD-binding_dom
IPR029061 THDP-binding
IPR012000 Thiamin_PyroP_enz_cen_dom
IPR012001 Thiamin_PyroP_enz_TPP-bd_dom
IPR000399 TPP-bd_CS
IPR011766 TPP_enzyme-bd_C
PfamiView protein in Pfam
PF02775 TPP_enzyme_C, 1 hit
PF00205 TPP_enzyme_M, 1 hit
PF02776 TPP_enzyme_N, 1 hit
SUPFAMiSSF52467 SSF52467, 1 hit
SSF52518 SSF52518, 2 hits
PROSITEiView protein in PROSITE
PS00187 TPP_ENZYMES, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07003-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKQTVAAYIA KTLESAGVKR IWGVTGDSLN GLSDSLNRMG TIEWMSTRHE
60 70 80 90 100
EVAAFAAGAE AQLSGELAVC AGSCGPGNLH LINGLFDCHR NHVPVLAIAA
110 120 130 140 150
HIPSSEIGSG YFQETHPQEL FRECSHYCEL VSSPEQIPQV LAIAMRKAVL
160 170 180 190 200
NRGVSVVVLP GDVALKPAPE GATMHWYHAP QPVVTPEEEE LRKLAQLLRY
210 220 230 240 250
SSNIALMCGS GCAGAHKELV EFAGKIKAPI VHALRGKEHV EYDNPYDVGM
260 270 280 290 300
TGLIGFSSGF HTMMNADTLV LLGTQFPYRA FYPTDAKIIQ IDINPASIGA
310 320 330 340 350
HSKVDMALVG DIKSTLRALL PLVEEKADRK FLDKALEDYR DARKGLDDLA
360 370 380 390 400
KPSEKAIHPQ YLAQQISHFA ADDAIFTCDV GTPTVWAARY LKMNGKRRLL
410 420 430 440 450
GSFNHGSMAN AMPQALGAQA TEPERQVVAM CGDGGFSMLM GDFLSVVQMK
460 470 480 490 500
LPVKIVVFNN SVLGFVAMEM KAGGYLTDGT ELHDTNFARI AEACGITGIR
510 520 530 540 550
VEKASEVDEA LQRAFSIDGP VLVDVVVAKE ELAIPPQIKL EQAKGFSLYM
560 570
LRAIISGRGD EVIELAKTNW LR
Length:572
Mass (Da):62,011
Last modified:April 1, 1988 - v1
Checksum:i57B38B9E3A92BDEA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti364 – 365QQ → HE in AAB59101 (PubMed:2663858).Curated2
Sequence conflicti364 – 365QQ → HE in AAB59102 (PubMed:2663858).Curated2
Sequence conflicti414 – 416QAL → HGV in AAB59101 (PubMed:2663858).Curated3
Sequence conflicti414 – 416QAL → HGV in AAB59102 (PubMed:2663858).Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
PIRiA23648 DEECPC
RefSeqiNP_415392.1, NC_000913.3
WP_000815337.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC73958; AAC73958; b0871
BAA35585; BAA35585; BAA35585
GeneIDi946132
KEGGiecj:JW0855
eco:b0871
PATRICifig|1411691.4.peg.1406

Similar proteinsi

Entry informationi

Entry nameiPOXB_ECOLI
AccessioniPrimary (citable) accession number: P07003
Secondary accession number(s): Q47513
, Q47514, Q47515, Q47516, Q47517, Q47518, Q47519, Q47520
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: March 28, 2018
This is version 157 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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