Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Pyruvate dehydrogenase [ubiquinone]

Gene

poxB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, Lipid-binding, Magnesium, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciEcoCyc:PYRUVOXID-MONOMER.
ECOL316407:JW0855-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10754. poxB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi533 – 5331A → T in poxB11. 1 Publication
Mutagenesisi549 – 57224Missing in poxB6. 1 PublicationAdd
BLAST
Mutagenesisi553 – 5531A → V in poxB14. 1 Publication
Mutagenesisi560 – 5601D → P in poxB15; normal activity. 1 Publication
Mutagenesisi564 – 5729Missing in poxB7. 1 Publication
Mutagenesisi564 – 5641E → P in poxB16; loss of activity. 1 Publication
Mutagenesisi570 – 5723Missing in poxB8. 1 Publication
Mutagenesisi572 – 5721R → G in poxB10; reduced activity; may interact less with membranes. 1 Publication

Chemistry

ChEMBLiCHEMBL3380.
DrugBankiDB00336. Nitrofural.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 572572Pyruvate dehydrogenase [ubiquinone]PRO_0000044606Add
BLAST
Peptidei550 – 57223Alpha-peptidePRO_0000035665Add
BLAST

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-2DPAGEP07003.

Interactioni

Subunit structurei

Homotetramer.1 Publication

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4262101. 12 interactions.
DIPiDIP-36216N.
IntActiP07003. 4 interactions.
STRINGi511145.b0871.

Structurei

Secondary structure

1
572
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1511Combined sources
Beta strandi20 – 234Combined sources
Helixi27 – 293Combined sources
Helixi30 – 3910Combined sources
Beta strandi41 – 466Combined sources
Helixi50 – 6415Combined sources
Beta strandi68 – 725Combined sources
Helixi76 – 794Combined sources
Helixi82 – 909Combined sources
Beta strandi95 – 1028Combined sources
Helixi104 – 1063Combined sources
Helixi117 – 1204Combined sources
Turni121 – 1244Combined sources
Beta strandi126 – 1305Combined sources
Helixi134 – 1363Combined sources
Helixi137 – 15014Combined sources
Beta strandi153 – 1608Combined sources
Helixi161 – 1644Combined sources
Beta strandi183 – 1853Combined sources
Helixi188 – 19912Combined sources
Beta strandi203 – 2086Combined sources
Helixi210 – 2123Combined sources
Helixi216 – 22611Combined sources
Beta strandi230 – 2323Combined sources
Helixi234 – 2363Combined sources
Helixi237 – 2404Combined sources
Beta strandi241 – 2433Combined sources
Beta strandi247 – 2504Combined sources
Helixi257 – 2659Combined sources
Beta strandi267 – 2737Combined sources
Helixi279 – 2813Combined sources
Beta strandi284 – 29310Combined sources
Helixi295 – 2973Combined sources
Beta strandi300 – 3023Combined sources
Beta strandi305 – 3095Combined sources
Helixi312 – 3198Combined sources
Helixi320 – 3223Combined sources
Helixi330 – 34819Combined sources
Beta strandi349 – 3513Combined sources
Beta strandi354 – 3574Combined sources
Helixi359 – 36911Combined sources
Beta strandi375 – 3784Combined sources
Helixi382 – 3909Combined sources
Beta strandi398 – 4003Combined sources
Turni403 – 4053Combined sources
Helixi411 – 42111Combined sources
Beta strandi427 – 4326Combined sources
Helixi433 – 4386Combined sources
Helixi440 – 4423Combined sources
Helixi443 – 4486Combined sources
Beta strandi454 – 4596Combined sources
Beta strandi461 – 4666Combined sources
Beta strandi468 – 4703Combined sources
Turni478 – 4803Combined sources
Helixi487 – 4937Combined sources
Beta strandi496 – 5016Combined sources
Helixi504 – 5063Combined sources
Helixi507 – 51610Combined sources
Beta strandi517 – 5193Combined sources
Beta strandi521 – 5277Combined sources
Helixi536 – 5427Combined sources
Turni543 – 5453Combined sources
Helixi548 – 5503Combined sources
Beta strandi551 – 5555Combined sources
Beta strandi559 – 5646Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EY9X-ray2.90A/B1-572[»]
3EYAX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L1-549[»]
ProteinModelPortaliP07003.
SMRiP07003. Positions 2-572.
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

Gene3Di3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR029035. 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.
[Graphical view]
PfamiPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
SUPFAMiSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
PROSITEiPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti364 – 3652QQ → HE in AAB59101 (PubMed:2663858).Curated
Sequence conflicti364 – 3652QQ → HE in AAB59102 (PubMed:2663858).Curated
Sequence conflicti414 – 4163QAL → HGV in AAB59101 (PubMed:2663858).Curated
Sequence conflicti414 – 4163QAL → HGV in AAB59102 (PubMed:2663858).Curated

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.
PATRICi32116949. VBIEscCol129921_0900.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EY9X-ray2.90A/B1-572[»]
3EYAX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L1-549[»]
ProteinModelPortaliP07003.
SMRiP07003. Positions 2-572.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262101. 12 interactions.
DIPiDIP-36216N.
IntActiP07003. 4 interactions.
STRINGi511145.b0871.

Chemistry

ChEMBLiCHEMBL3380.
DrugBankiDB00336. Nitrofural.

2D gel databases

SWISS-2DPAGEP07003.

Proteomic databases

EPDiP07003.
PaxDbiP07003.
PRIDEiP07003.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73958; AAC73958; b0871.
BAA35585; BAA35585; BAA35585.
GeneIDi946132.
KEGGiecj:JW0855.
eco:b0871.
PATRICi32116949. VBIEscCol129921_0900.

Organism-specific databases

EchoBASEiEB0747.
EcoGeneiEG10754. poxB.

Phylogenomic databases

eggNOGiENOG4105C7K. Bacteria.
COG0028. LUCA.
InParanoidiP07003.
KOiK00156.
OMAiRGKEWIQ.
PhylomeDBiP07003.

Enzyme and pathway databases

BioCyciEcoCyc:PYRUVOXID-MONOMER.
ECOL316407:JW0855-MONOMER.
MetaCyc:PYRUVOXID-MONOMER.
BRENDAi1.2.5.1. 2026.

Miscellaneous databases

EvolutionaryTraceiP07003.
PROiP07003.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR029035. 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.
[Graphical view]
PfamiPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
SUPFAMiSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
PROSITEiPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPOXB_ECOLI
AccessioniPrimary (citable) accession number: P07003
Secondary accession number(s): Q47513
, Q47514, Q47515, Q47516, Q47517, Q47518, Q47519, Q47520
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: September 7, 2016
This is version 147 of the entry and version 1 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.