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Database: UniProt
Entry: V6Z2N0_STRAG
LinkDB: V6Z2N0_STRAG
Original site: V6Z2N0_STRAG 
ID   V6Z2N0_STRAG            Unreviewed;       593 AA.
AC   V6Z2N0;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Pyruvate oxidase {ECO:0000313|EMBL:ESV53839.1};
GN   ORFNames=SAG0136_00880 {ECO:0000313|EMBL:ESV53839.1};
OS   Streptococcus agalactiae LMG 14747.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1154860 {ECO:0000313|EMBL:ESV53839.1, ECO:0000313|Proteomes:UP000018482};
RN   [1] {ECO:0000313|EMBL:ESV53839.1, ECO:0000313|Proteomes:UP000018482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 14747 {ECO:0000313|EMBL:ESV53839.1,
RC   ECO:0000313|Proteomes:UP000018482};
RA   Richards V.P., Durkin S.A.S., Kim M., Pavinski Bitar P.D., Stanhope M.J.,
RA   Town C.D., Venter J.C.;
RL   Submitted (MAY-2013) 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:ESV53839.1}.
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DR   EMBL; ANQC01000012; ESV53839.1; -; Genomic_DNA.
DR   AlphaFoldDB; V6Z2N0; -.
DR   eggNOG; COG0028; Bacteria.
DR   Proteomes; UP000018482; Unassembled WGS sequence.
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:ESV53839.1};
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..327
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   593 AA;  65610 MW;  6E7D80F684AB8687 CRC64;
     MSNGKITASA AMLNVLKTWG VDTIYGIPSG TLSSLMDALA EDKDINFLQV RHEETGSLAA
     LMQAKFGGSI GVCVGSGGPG ATHLINGIYD AAMDATPMLA ILGSRPVNEL NMDAFQELNQ
     NPMYNGIAVF NKRVAYAEQL PKVIDDAVRA AIAKKGPAVV EIPVNFGFQE IDEDSYYGSG
     EFDRTFVAPG LNEVEISKAV EILNAAERPV IYSGFGGRGA GEIITELSRK LKAPVITTGK
     NFETFEWNYE GLTGSAYRVG WKPANEVVFE ADTVLFLGCN FPFSEVYNTF KNTEKFIQVD
     IDPYKLGKRH ALDASILGDV KEAAKALLER VDIVEESAWW NAAVKNNQNW RNYMNKLEGK
     TEGALQLYQV YNAINKYADE DAIYSIDVGN STQTSTRHLH MTPKNMWRTS PLFATMGIAL
     PGGIAAKKDN PDRQVWNIMG DGAFGMCYPD VITNVQYNLP VINIVFSNAE YAFIKNKYED
     TNKHLFGVDF TNPDYVKIAE AQGAVGFRVE RIEDMDAVMK EAVELNKAGR TIVIDARITQ
     DRPIPVEAPI MTLDPKLFSE QEIADFKVKY EAEELVPFRE FLEAEGLESR YIK
//
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