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P37063 (POXB_LACPL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pyruvate oxidase
EC=1.2.3.3
Alternative name(s):
Pyruvic oxidase
Short name=POX
Gene names
Name:pox5
Ordered Locus Names:lp_3589
OrganismLactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
Taxonomic identifier220668 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein attributes

Sequence length603 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Important for the aerobic growth. Decarboxylates pyruvate in four steps. The energy released is partially stored in acetyl phosphate.

Catalytic activity

Pyruvate + phosphate + O2 = acetyl phosphate + CO2 + H2O2.

Cofactor

Binds 1 FAD per subunit.

Binds 1 magnesium ion per subunit.

Binds 1 thiamine pyrophosphate per subunit.

Subunit structure

Homotetramer.

Domain

Each monomer is divided into three domains, each of which contains a six-stranded parallel beta sheet surrounded by alpha helices.

Sequence similarities

Belongs to the TPP enzyme family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 603603Pyruvate oxidase
PRO_0000090818

Regions

Domain192 – 342151FAD-binding
Region1 – 191191Core
Region343 – 603261Thiamine pyrophosphate binding

Sites

Metal binding4471Magnesium
Metal binding4741Magnesium
Metal binding4761Magnesium

Secondary structure

1 ........................................................................................................... 603
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P37063 [UniParc].

Last modified March 25, 2003. Version 3.
Checksum: 71BEDD006EEB0FBE

FASTA60366,111
        10         20         30         40         50         60 
MVMKQTKQTN ILAGAAVIKV LEAWGVDHLY GIPGGSINSI MDALSAERDR IHYIQVRHEE 

        70         80         90        100        110        120 
VGAMAAAADA KLTGKIGVCF GSAGPGGTHL MNGLYDARED HVPVLALIGQ FGTTGMNMDT 

       130        140        150        160        170        180 
FQEMNENPIY ADVADYNVTA VNAATLPHVI DEAIRRAYAH QGVAVVQIPV DLPWQQIPAE 

       190        200        210        220        230        240 
DWYASANSYQ TPLLPEPDVQ AVTRLTQTLL AAERPLIYYG IGARKAGKEL EQLSKTLKIP 

       250        260        270        280        290        300 
LMSTYPAKGI VADRYPAYLG SANRVAQKPA NEALAQADVV LFVGNNYPFA EVSKAFKNTR 

       310        320        330        340        350        360 
YFLQIDIDPA KLGKRHKTDI AVLADAQKTL AAILAQVSER ESTPWWQANL ANVKNWRAYL 

       370        380        390        400        410        420 
ASLEDKQEGP LQAYQVLRAV NKIAEPDAIY SIDVGDINLN ANRHLKLTPS NRHITSNLFA 

       430        440        450        460        470        480 
TMGVGIPGAI AAKLNYPERQ VFNLAGDGGA SMTMQDLATQ VQYHLPVINV VFTNCQYGFI 

       490        500        510        520        530        540 
KDEQEDTNQN DFIGVEFNDI DFSKIADGVH MQAFRVNKIE QLPDVFEQAK AIAQHEPVLI 

       550        560        570        580        590        600 
DAVITGDRPL PAEKLRLDSA TSSAADIEAF KQRYEAQDLQ PLSTYLKQFG LDDLQHQIGQ 


GGF

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Lactobacillus plantarum WCFS1."
Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P., Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J., Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M., Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M., Siezen R.J.
Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003) [PubMed: 12566566] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-793 / NCIMB 8826 / WCFS1.
[2]"The refined structures of a stabilized mutant and of wild-type pyruvate oxidase from Lactobacillus plantarum."
Muller Y.A., Schumacher G., Rudolph R., Schulz G.E.
J. Mol. Biol. 237:315-335(1994) [PubMed: 8145244] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 AND 2.1 ANGSTROMS) OF WILD-TYPE AND MUTANT.
[3]"Structure of the thiamine- and flavin-dependent enzyme pyruvate oxidase."
Muller Y.A., Schulz G.E.
Science 259:965-967(1993) [PubMed: 8438155] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL935263 Genomic DNA. Translation: CCC80550.1.
RefSeqNP_786788.1. NC_004567.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1POWX-ray2.50A/B9-593[»]
1POXX-ray2.10A/B9-593[»]
1Y9DX-ray2.20A/B/C/D1-603[»]
2EZ4X-ray2.03A/B1-603[»]
2EZ8X-ray1.96A/B1-603[»]
2EZ9X-ray1.60A/B1-603[»]
2EZTX-ray2.29A/B1-603[»]
2EZUX-ray2.16A/B1-603[»]
ProteinModelPortalP37063.
SMRP37063. Positions 9-593.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1062065.
GenomeReviewsGene locus lp_3589 in contig AL935263_GR.
KEGGlpl:lp_3589.
NMPDRfig|220668.1.peg.2922.
PATRIC22252792. VBILacPla27411_2994.

Phylogenomic databases

HOGENOMHBG323037.
OMAWYASANS.
ProtClustDBCLSK2520657.

Enzyme and pathway databases

BioCycLPLA220668:LP_3589-MONOMER.

Family and domain databases

InterProIPR014092. Pyruvate_oxidase.
IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR000399. TPP-bd_CS.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]
KOK00158.
PfamPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR02720. Pyruv_oxi_spxB. 1 hit.
PROSITEPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePOXB_LACPL
AccessionPrimary (citable) accession number: P37063
Secondary accession number(s): F9ULE3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: March 25, 2003
Last modified: January 25, 2012
This is version 91 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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