[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1; DOI=10.1073/pnas.0337704100; PubMed=12566566 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Complete genome sequence of Lactobacillus plantarum WCFS1."; Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
[2]	X-RAY CRYSTALLOGRAPHY (2.5 AND 2.1 ANGSTROMS) OF WILD-TYPE AND MUTANT. DOI=10.1006/jmbi.1994.1233; PubMed=8145244 [NCBI, ExPASy, EBI, Israel, Japan] Muller Y.A., Schumacher G., Rudolph R., Schulz G.E.; "The refined structures of a stabilized mutant and of wild-type pyruvate oxidase from Lactobacillus plantarum."; J. Mol. Biol. 237:315-335(1994).
[3]	X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). PubMed=8438155 [NCBI, ExPASy, EBI, Israel, Japan] Muller Y.A., Schulz G.E.; "Structure of the thiamine- and flavin-dependent enzyme pyruvate oxidase."; Science 259:965-967(1993).

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.
COFACTOR: Binds 1 magnesium ion per subunit.
COFACTOR: Binds 1 thiamine pyrophosphate per subunit.
SUBUNIT: Homotetramer.
DOMAIN: Each monomer is divided into three domains, each of which contains a six-stranded parallel beta sheet surrounded by alpha helices.
SIMILARITY: Belongs to the TPP enzyme family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AL935262; CAD65666.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_786788.1; -.

3D structure databases

PDB

1POW; X-ray; 2.50 A; A/B=9-593.	[ExPASy / RCSB / EBI]
1POX; X-ray; 2.10 A; A/B=9-593.	[ExPASy / RCSB / EBI]
1Y9D; X-ray; 2.20 A; A/B/C/D=1-603.	[ExPASy / RCSB / EBI]
2EZ4; X-ray; 2.03 A; A/B=1-603.	[ExPASy / RCSB / EBI]
2EZ8; X-ray; 1.96 A; A/B=1-603.	[ExPASy / RCSB / EBI]
2EZ9; X-ray; 1.60 A; A/B=1-603.	[ExPASy / RCSB / EBI]
2EZT; X-ray; 2.29 A; A/B=1-603.	[ExPASy / RCSB / EBI]
2EZU; X-ray; 2.16 A; A/B=1-603.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1POW; -.
1POX; -.
1Y9D; -.
2EZ4; -.
2EZ8; -.
2EZ9; -.
2EZT; -.
2EZU; -.

ModBase

P37063.

Enzyme and pathway databases

BioCyc

LPLA220668:LP_3589-MON; -.

Ontologies

GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from InterPro).
GO:0047112;	Molecular function: pyruvate oxidase activity (inferred from electronic annotation from EC).
GO:0030976;	Molecular function: thiamin pyrophosphate binding (inferred from electronic annotation from InterPro).
GO:0016740;	Molecular function: transferase activity (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR014092; Pyruvate_oxidase.
IPR000399; TPP_bd_CS.
IPR012001; TPP_bd_enzyme_N.
IPR011766; TPP_enzyme_bd_C.
IPR012000; TPP_enzyme_M.
Graphical view of domain structure.

Pfam

PF02775; TPP_enzyme_C; 1.
PF00205; TPP_enzyme_M; 1.
PF02776; TPP_enzyme_N; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR02720; pyruv_oxi_spxB; 1.

PROSITE

PS00187; TPP_ENZYMES; 1.

ProtoNet

P37063.

Genome annotation databases

GeneID

1062065; -.

GenomeReviews

AL935263_GR; lp_3589.

KEGG

lpl:lp_3589; -.

NMPDR

fig|220668.1.peg.2922; -.

Phylogenomic databases

HOGENOM

P37063; -.

Other

LinkHub

P37063; -.

Genome annotation databases

CMR

P37063; lp_3589.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Complete proteome; FAD; Flavoprotein; Magnesium; Metal-binding; Oxidoreductase; Thiamine pyrophosphate.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 603`	`603`	`Pyruvate oxidase.`	`PRO_0000090818`
`DOMAIN`	`192 342`	`151`	`FAD-binding.`
`REGION`	`1 191`	`191`	`Core.`
`REGION`	`343 603`	`261`	`Thiamine pyrophosphate binding.`
`METAL`	`447 447`		`Magnesium.`
`METAL`	`474 474`		`Magnesium.`
`METAL`	`476 476`		`Magnesium.`
`STRAND`	`10 12`	`3`
`HELIX`	`13 23`	`11`
`STRAND`	`28 31`	`4`
`HELIX`	`35 37`	`3`
`HELIX`	`38 46`	`9`
`TURN`	`47 50`	`4`
`STRAND`	`51 55`	`5`
`HELIX`	`59 73`	`15`
`STRAND`	`77 81`	`5`
`HELIX`	`85 88`	`4`
`HELIX`	`91 99`	`9`
`STRAND`	`104 110`	`7`
`TURN`	`113 117`	`5`
`HELIX`	`127 130`	`4`
`TURN`	`131 133`	`3`
`STRAND`	`135 139`	`5`
`HELIX`	`146 160`	`15`
`STRAND`	`162 169`	`8`
`HELIX`	`172 174`	`3`
`STRAND`	`175 178`	`4`
`HELIX`	`186 188`	`3`
`HELIX`	`199 211`	`13`
`STRAND`	`213 219`	`7`
`HELIX`	`221 226`	`6`
`HELIX`	`227 237`	`11`
`STRAND`	`241 243`	`3`
`HELIX`	`245 247`	`3`
`STRAND`	`263 266`	`4`
`HELIX`	`268 276`	`9`
`STRAND`	`278 284`	`7`
`TURN`	`288 298`	`11`
`STRAND`	`300 307`	`8`
`HELIX`	`309 311`	`3`
`STRAND`	`314 316`	`3`
`STRAND`	`319 324`	`6`
`HELIX`	`326 336`	`11`
`HELIX`	`344 364`	`21`
`STRAND`	`368 370`	`3`
`HELIX`	`373 383`	`11`
`STRAND`	`389 392`	`4`
`HELIX`	`396 404`	`9`
`STRAND`	`412 414`	`3`
`HELIX`	`425 435`	`11`
`STRAND`	`441 446`	`6`
`HELIX`	`447 453`	`7`
`HELIX`	`454 456`	`3`
`HELIX`	`457 462`	`6`
`STRAND`	`468 473`	`6`
`HELIX`	`478 487`	`10`
`STRAND`	`494 496`	`3`
`HELIX`	`502 509`	`8`
`STRAND`	`512 516`	`5`
`HELIX`	`519 521`	`3`
`HELIX`	`522 532`	`11`
`TURN`	`533 535`	`3`
`STRAND`	`538 543`	`6`
`TURN`	`559 561`	`3`
`HELIX`	`564 574`	`11`
`HELIX`	`582 588`	`7`

Sequence information

Length: 603 AA [This is the length of the unprocessed precursor]

Molecular weight: 66111 Da [This is the MW of the unprocessed precursor]

CRC64: 71BEDD006EEB0FBE [This is a checksum on the sequence]

        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

P37063 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools