ID W9EN21_9LACO Unreviewed; 605 AA.
AC W9EN21;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Pyruvate oxidase {ECO:0000313|EMBL:ETO41054.1};
GN ORFNames=B808_15 {ECO:0000313|EMBL:ETO41054.1};
OS Fructilactobacillus florum 8D.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Fructilactobacillus.
OX NCBI_TaxID=1221538 {ECO:0000313|EMBL:ETO41054.1, ECO:0000313|Proteomes:UP000019474};
RN [1] {ECO:0000313|EMBL:ETO41054.1, ECO:0000313|Proteomes:UP000019474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8D {ECO:0000313|EMBL:ETO41054.1,
RC ECO:0000313|Proteomes:UP000019474};
RA Kim E.B., Marco M.L.;
RT "Genome sequencing of Lactobacillus florum 8D.";
RL Submitted (AUG-2012) 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:ETO41054.1}.
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DR EMBL; ALXG01000002; ETO41054.1; -; Genomic_DNA.
DR RefSeq; WP_009167292.1; NZ_ALXG01000002.1.
DR AlphaFoldDB; W9EN21; -.
DR PATRIC; fig|1221538.3.peg.15; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000019474; 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; 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:ETO41054.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019474};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 11..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 200..328
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 389..538
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 605 AA; 65919 MW; A429AE7D5AC55C04 CRC64;
MTDVKKIPAA VAMVKVLEAY GVKDVYGYPG GSINSTLHAL DAEKDNINYI QVRHEQVGAL
AASAHAKLTG KLGVAFGSAG PGAVNLLNGL YDAKEDHAPV LALVGQVPHN NMNYNYFQEM
PEVPIFEDVS VYNRIVMTPE SLPHVIDRAI HEAYQKKGVA VVVIPNDFGF AEIPDVRYDS
ASATYDKPAP QPVASDAEVD AFLELVHEAK RPVIHVGRGI KAGGEKLVEL SRKLQIPFIF
DGLAKGTLDE DYEGNLGTAN RAASKAADEI LSTADLVIAI GGDFPFANSV YASHEFKYIQ
IDNQAVELGR HHVPELSILS DATKFVEKAL ERSQKVAPSA FFQAAAADMQ NWKAYIHKML
TSQSDPLLPA QVYNQVNRIA EKDAIFSVDV GDNIINTFRY LDVKPAQKWV ISALFATMGS
GVPGAIAAKQ NDPTKQVFNI AGDGALSMVM QDLVTEVKYK LPIINIVTQN GNLGFIEGEQ
EDLPMQIFGL DLQKQNFAMI AKGMGLDAVR VKNYAELPAA FDEALMALKA GKPFLIDIEI
DKTRGLPVED LIVKIKDGKL SETVSPNYLK NKGKGAYTLD EFFAKYDGQE LKPLAHFFDE
AGVRL
//
