ID B2INB2_STRPS Unreviewed; 591 AA.
AC B2INB2;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Pyruvate oxidase {ECO:0000313|EMBL:ACB89931.1};
GN Name=spxB {ECO:0000313|EMBL:ACB89931.1};
GN OrderedLocusNames=SPCG_0679 {ECO:0000313|EMBL:ACB89931.1};
OS Streptococcus pneumoniae (strain CGSP14).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=516950 {ECO:0000313|EMBL:ACB89931.1, ECO:0000313|Proteomes:UP000001682};
RN [1] {ECO:0000313|EMBL:ACB89931.1, ECO:0000313|Proteomes:UP000001682}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGSP14 {ECO:0000313|EMBL:ACB89931.1,
RC ECO:0000313|Proteomes:UP000001682};
RX PubMed=19361343; DOI=10.1186/1471-2164-10-158;
RA Ding F., Tang P., Hsu M.-H., Cui P., Hu S., Yu J., Chiu C.-H.;
RT "Genome evolution driven by host adaptations results in a more virulent and
RT antimicrobial-resistant Streptococcus pneumoniae serotype 14.";
RL BMC Genomics 10:158-158(2009).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP001033; ACB89931.1; -; Genomic_DNA.
DR RefSeq; WP_000191795.1; NC_010582.1.
DR AlphaFoldDB; B2INB2; -.
DR SMR; B2INB2; -.
DR KEGG; spw:SPCG_0679; -.
DR HOGENOM; CLU_013748_3_0_9; -.
DR Proteomes; UP000001682; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0047112; F:pyruvate oxidase activity; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd02014; TPP_POX; 1.
DR CDD; cd07039; TPP_PYR_POX; 1.
DR Gene3D; 1.10.10.940; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR047211; POXB-like.
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_TPP-bd.
DR InterPro; IPR047212; TPP_POXB-like.
DR InterPro; IPR047210; TPP_PYR_POXB-like.
DR NCBIfam; TIGR02720; pyruv_oxi_spxB; 1.
DR PANTHER; PTHR42981; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR PANTHER; PTHR42981:SF2; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Pyruvate {ECO:0000313|EMBL:ACB89931.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 7..122
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 196..326
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 387..535
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 591 AA; 65280 MW; 0262084452611868 CRC64;
MTQGKITASA AMLNVLKTWG VDTIYGIPSG TLSSLMDALA EDKDIRFLQV RHEETGALAA
VMQAKFGGSI GVAVGSGGPG ATHLINGVYD AAMDNTPFLA ILGSRPVNEL NMDAFQELNQ
NPMYNGIAVY NKRVAYAEQL PKVIDEACRA AISKKGPAVV 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
//
