POXB_STRPN
ID POXB_STRPN Reviewed; 591 AA.
AC Q54970;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Pyruvate oxidase;
DE EC=1.2.3.3;
DE AltName: Full=Pyruvic oxidase;
DE Short=POX;
GN Name=spxB; OrderedLocusNames=SP_0730;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=R6x;
RX PubMed=8820650; DOI=10.1046/j.1365-2958.1996.425954.x;
RA Spellerberg B., Cundell D.R., Sandros J., Pearce B.J.,
RA Idanpaan-Heikkila I., Rosenow C., Masure H.R.;
RT "Pyruvate oxidase, as a determinant of virulence in Streptococcus
RT pneumoniae.";
RL Mol. Microbiol. 19:803-813(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
CC -!- FUNCTION: Important for the aerobic growth. Decarboxylates pyruvate in
CC four steps. The energy released is partially stored in acetyl phosphate
CC (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + O2 + phosphate + pyruvate = acetyl phosphate + CO2 +
CC H2O2; Xref=Rhea:RHEA:20848, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:22191, ChEBI:CHEBI:43474; EC=1.2.3.3;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR EMBL; L39074; AAB40976.1; -; Genomic_DNA.
DR EMBL; AE005672; AAK74871.1; -; Genomic_DNA.
DR PIR; F95084; F95084.
DR RefSeq; WP_000191798.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; Q54970; -.
DR SMR; Q54970; -.
DR STRING; 170187.SP_0730; -.
DR PRIDE; Q54970; -.
DR EnsemblBacteria; AAK74871; AAK74871; SP_0730.
DR GeneID; 66805871; -.
DR KEGG; spn:SP_0730; -.
DR eggNOG; COG0028; Bacteria.
DR OMA; AANWYAR; -.
DR PhylomeDB; Q54970; -.
DR BioCyc; SPNE170187:G1FZB-749-MON; -.
DR BRENDA; 1.2.3.3; 1960.
DR PHI-base; PHI:3604; -.
DR Proteomes; UP000000585; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0047112; F:pyruvate oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR014092; Pyruvate_oxidase.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR011766; TPP_enzyme-bd_C.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR TIGRFAMs; TIGR02720; pyruv_oxi_spxB; 1.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Magnesium; Metal-binding; Oxidoreductase;
KW Thiamine pyrophosphate.
FT CHAIN 1..591
FT /note="Pyruvate oxidase"
FT /id="PRO_0000090819"
FT REGION 1..188
FT /note="Core"
FT REGION 189..336
FT /note="FAD-binding"
FT REGION 337..591
FT /note="Thiamine pyrophosphate binding"
FT BINDING 441
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 468
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 470
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CONFLICT 152
FT /note="V -> I (in Ref. 1; AAB40976)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="P -> A (in Ref. 1; AAB40976)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="I -> L (in Ref. 1; AAB40976)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="N -> S (in Ref. 1; AAB40976)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="N -> T (in Ref. 1; AAB40976)"
FT /evidence="ECO:0000305"
FT CONFLICT 496
FT /note="A -> G (in Ref. 1; AAB40976)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="E -> G (in Ref. 1; AAB40976)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 591 AA; 65266 MW; DCF1595F7485B6FD CRC64;
MTQGKITASA AMLNVLKTWG VDTIYGIPSG TLSSLMDALA EDKDIRFLQV RHEETGALAA
VMQAKFGGSI GVAVGSGGPG ATHLINGVYD AAMDNTPFLA ILGSRPVNEL NMDAFQELNQ
NPMYNGIAVY NKRVAYAEQL PKVIDEACRA AVSKKGPAVV EIPVNFGFQE IDENSYYGSG
SYERSFIAPA LNEVEIDKAV EILNNAERPV IYAGFGGVKA GEVITELSRK IKAPIITTGK
NFEAFEWNYE GLTGSAYRVG WKPANEVVFE ADTVLFLGSN FPFAEVYEAF KNTEKFIQVD
IDPYKLGKRH ALDASILGDA GQAAKAILDK VNPVESTPWW RANVKNNQNW RDYMNKLEGK
TEGELQLYQV YNAINKHADQ DAIYSIDVGN TTQTSTRHLH MTPKNMWRTS PLFATMGIAL
PGGIAAKKDN PDRQVWNIMG DGAFNMCYPD VITNVQYDLP VINLVFSNAE YGFIKNKYED
TNKHLFGVDF TNADYAKIAE AQGAVGFTVD RIEDIDAVVA EAVKLNKEGK TVVIDARITQ
HRPLPVEVLE LDPKLHSEEA IKAFKEKYEA EELVPFRLFL EEEGLQSRAI K
