NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=R6x;
PubMed=8820650 [NCBI, ExPASy, EBI, Israel, Japan]
Spellerberg B., Cundell D.R., Sandros J., Pearce B.J., Idanpaan-Heikkila I., Rosenow C., Masure H.R.;
"Pyruvate oxidase, as a determinant of virulence in Streptococcus pneumoniae.";
Mol. Microbiol. 19:803-813(1996).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-334 / TIGR4;
DOI=10.1126/science.1061217; PubMed=11463916 [NCBI, ExPASy, EBI, Israel, Japan]
Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D., Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J., Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D., Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D., Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L., McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K., Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A., Morrison D.A., Hollingshead S.K., Fraser C.M.;
"Complete genome sequence of a virulent isolate of Streptococcus pneumoniae.";
Science 293:498-506(2001).

Comments

FUNCTION: Important for the aerobic growth. Decarboxylates pyruvate in four steps. The energy released is partially stored in acetyl phosphate (By similarity).
CATALYTIC ACTIVITY: Pyruvate + phosphate + O₂ = acetyl phosphate + CO₂ + H₂O₂.
COFACTOR: Binds 1 FAD per subunit (By similarity).
COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
COFACTOR: Binds 1 thiamine pyrophosphate per subunit (By similarity).
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

L39074; AAB40976.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE005672; AAK74871.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

F95084; F95084.

RefSeq

NP_345231.1; -.

3D structure databases

HSSP

P37063; 1POX. [HSSP ENTRY / PDB]

ModBase

Q54970.

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.

BLOCKS

Q54970.

Genome annotation databases

GeneID

930680; -.

GenomeReviews

AE005672_GR; SP_0730.

KEGG

spn:SP_0730; -.

TIGR

SP_0730; -.

Phylogenomic databases

HOGENOM

Q54970; -.

Other

ProtoNet

Q54970.

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 591`	`591`	`Pyruvate oxidase.`	`PRO_0000090819`
`DOMAIN`	`189 336`	`148`	`FAD-binding.`
`REGION`	`1 188`	`188`	`Core.`
`REGION`	`337 591`	`255`	`Thiamine pyrophosphate binding.`
`METAL`	`441 441`		`Magnesium (By similarity).`
`METAL`	`468 468`		`Magnesium (By similarity).`
`METAL`	`470 470`		`Magnesium (By similarity).`
`CONFLICT`	`152 152`		`V -> I (in Ref. 1; AAB40976).`
`CONFLICT`	`282 282`		`P -> A (in Ref. 1; AAB40976).`
`CONFLICT`	`386 386`		`I -> L (in Ref. 1; AAB40976).`
`CONFLICT`	`390 390`		`N -> S (in Ref. 1; AAB40976).`
`CONFLICT`	`430 430`		`N -> T (in Ref. 1; AAB40976).`
`CONFLICT`	`496 496`		`A -> G (in Ref. 1; AAB40976).`
`CONFLICT`	`528 528`		`E -> G (in Ref. 1; AAB40976).`

Sequence information

Length: 591 AA [This is the length of the unprocessed precursor]

Molecular weight: 65266 Da [This is the MW of the unprocessed precursor]

CRC64: DCF1595F7485B6FD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTQGKITASA AMLNVLKTWG VDTIYGIPSG TLSSLMDALA EDKDIRFLQV RHEETGALAA 

        70         80         90        100        110        120 
VMQAKFGGSI GVAVGSGGPG ATHLINGVYD AAMDNTPFLA ILGSRPVNEL NMDAFQELNQ 

       130        140        150        160        170        180 
NPMYNGIAVY NKRVAYAEQL PKVIDEACRA AVSKKGPAVV EIPVNFGFQE IDENSYYGSG 

       190        200        210        220        230        240 
SYERSFIAPA LNEVEIDKAV EILNNAERPV IYAGFGGVKA GEVITELSRK IKAPIITTGK 

       250        260        270        280        290        300 
NFEAFEWNYE GLTGSAYRVG WKPANEVVFE ADTVLFLGSN FPFAEVYEAF KNTEKFIQVD 

       310        320        330        340        350        360 
IDPYKLGKRH ALDASILGDA GQAAKAILDK VNPVESTPWW RANVKNNQNW RDYMNKLEGK 

       370        380        390        400        410        420 
TEGELQLYQV YNAINKHADQ DAIYSIDVGN TTQTSTRHLH MTPKNMWRTS PLFATMGIAL 

       430        440        450        460        470        480 
PGGIAAKKDN PDRQVWNIMG DGAFNMCYPD VITNVQYDLP VINLVFSNAE YGFIKNKYED 

       490        500        510        520        530        540 
TNKHLFGVDF TNADYAKIAE AQGAVGFTVD RIEDIDAVVA EAVKLNKEGK TVVIDARITQ 

       550        560        570        580        590 
HRPLPVEVLE LDPKLHSEEA IKAFKEKYEA EELVPFRLFL EEEGLQSRAI K

Q54970 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