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
//