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Database: UniProt
Entry: A0A0D1A6Q9_9LACO
LinkDB: A0A0D1A6Q9_9LACO
Original site: A0A0D1A6Q9_9LACO 
ID   A0A0D1A6Q9_9LACO        Unreviewed;       581 AA.
AC   A0A0D1A6Q9;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Pyruvate oxidase {ECO:0000313|EMBL:KIS03402.1};
DE            EC=1.2.3.3 {ECO:0000313|EMBL:KIS03402.1};
GN   Name=poxB {ECO:0000313|EMBL:KIS03402.1};
GN   ORFNames=WDC_0981 {ECO:0000313|EMBL:KIS03402.1};
OS   Paucilactobacillus wasatchensis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Paucilactobacillus.
OX   NCBI_TaxID=1335616 {ECO:0000313|EMBL:KIS03402.1, ECO:0000313|Proteomes:UP000032279};
RN   [1] {ECO:0000313|EMBL:KIS03402.1, ECO:0000313|Proteomes:UP000032279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WDC04 {ECO:0000313|EMBL:KIS03402.1,
RC   ECO:0000313|Proteomes:UP000032279};
RA   Oberg C.J., Culumber M., McMahon D.J., Broadbent J.R., Oberg T.S.,
RA   Ortaki F.;
RT   "Lactobacillus wasatchii sp. WDC04, a late gas producing bacteria isolated
RT   from aged chedder cheese.";
RL   Submitted (AUG-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:KIS03402.1}.
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DR   EMBL; AWTT01000020; KIS03402.1; -; Genomic_DNA.
DR   RefSeq; WP_044010729.1; NZ_AWTT01000020.1.
DR   AlphaFoldDB; A0A0D1A6Q9; -.
DR   STRING; 1335616.WDC_0981; -.
DR   PATRIC; fig|1335616.4.peg.984; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000032279; 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:KIS03402.1};
KW   Pyruvate {ECO:0000313|EMBL:KIS03402.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032279};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          6..120
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          196..325
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          385..531
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   581 AA;  63261 MW;  0BBA2AA98C8046E6 CRC64;
     MTNKINAADA MIKVLEDWQI DHIFGLPGGS FDSTMNALYN RQNSIKYVQV RHEETGALAA
     AGEAKFTGKI GVTFGSAGPG AVHLLNGLYD AKHDGVPVLA LVGQVGTDFM NTEYFQELNE
     NPIFADVAVY NRTVMTAEQL PAVVDQAIRQ AYEHSGVAVV TIPKDLGWAE IDDDYISTAG
     NYAVTENYPL PDKVAVKQAA EILQNAKRPV IYFGLGAKKA GPELKRLSDR LKIPLMSSAL
     AKGVIADDDP AYMGSAGRVA TKPGVETARA ADAILFIGSN FPFAAYFFSP TAKFIQVDVK
     PTNIGKRHHV DVGILADAKT TLTALTNQVE EVGKRAFYEA ALANKREWRD WLAKFVDEDK
     QPLNVDSVFE QINRIATDDA IFALDVGNVT IDGVRLLQMK PTQKMATSGW YATMGFALPA
     AIGAQFSYPN RQVFSISGDG GYTMVMHDIL TQVKYQQPII NVVLTNQSLG FIEAEQDDTK
     QPHSGVDLID ANFGAAATDM GATGYEVHTL SELHQAFDDA KSTNGPVVID VKIANDRPLP
     VEQLVLTTDD QHSQTDVDQF IKQYHAEGLT PFSEFLAQYK A
//
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