ID F2BUI6_STRSA Unreviewed; 591 AA.
AC F2BUI6;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Pyruvate oxidase {ECO:0000313|EMBL:EGF05377.1};
DE EC=1.2.3.3 {ECO:0000313|EMBL:EGF05377.1};
GN Name=spxB {ECO:0000313|EMBL:EGF05377.1};
GN ORFNames=HMPREF9394_2088 {ECO:0000313|EMBL:EGF05377.1};
OS Streptococcus sanguinis SK1057.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=888821 {ECO:0000313|EMBL:EGF05377.1, ECO:0000313|Proteomes:UP000005977};
RN [1] {ECO:0000313|EMBL:EGF05377.1, ECO:0000313|Proteomes:UP000005977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK1057 {ECO:0000313|EMBL:EGF05377.1,
RC ECO:0000313|Proteomes:UP000005977};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGF05377.1}.
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DR EMBL; AFBA01000010; EGF05377.1; -; Genomic_DNA.
DR RefSeq; WP_004188735.1; NZ_GL878514.1.
DR AlphaFoldDB; F2BUI6; -.
DR PATRIC; fig|888821.3.peg.2053; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_0_9; -.
DR Proteomes; UP000005977; Unassembled WGS sequence.
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 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 Oxidoreductase {ECO:0000313|EMBL:EGF05377.1};
KW Pyruvate {ECO:0000313|EMBL:EGF05377.1};
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; 65254 MW; D5FE3E57763EB490 CRC64;
MTQGKITASA AMLNVLKTWG VDTIYGIPSG TLSSLMDALA EDKDIRFLQV RHEETGALAA
VMQAKFGGSI GVAVGSGGPG ATHLINGVYD AAMDNTPFLA ILGSRPVNEL NMDAFQELNQ
NPMYNGIAVY NKRVAYAEQL PKVIDEACRA AVSKKGPAVV EIPVNFGFQE INENSYYGSG
SYERSFIAPA LNETEIDKAV EILNKAERPV IYAGFGGVKA GEVITELSRK IKAPIITTGK
NFEAFEWNYE GLTGSAYRVG WKPANEVVFE ADTVLFLGSN FPFAEVYEAF KNTEKFIQVD
IDPYKLGKRH ALDASILGDA GQAAKAILDK VDAVVSTPWW RANVKNNQNW RDYMNKLEGK
TEGELQLYQV YNAVNKYADQ DAIYSIDVGN TTQTSTRHLH MTPKNMWRTS PLFATMGIAL
PGGIAAKKDN PDRQVWNIMG DGAFNMCYPD VITNVQYDLP VINLVFSNAE YGFIKNKYED
TNKHLFGVDF TNADYAKIAE AQGAVGFTVD RIEDIDAVVA EAVKLNKEGK TVVIDARITQ
HRPLPVEVLE LDPKLHSEEA IKSFKEKYEA EELVPFRLFL EEEGLQSRAI K
//
