ID W6T6Y2_9LACO Unreviewed; 583 AA.
AC W6T6Y2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Pyruvate oxidase {ECO:0000313|EMBL:ETY74006.1};
GN ORFNames=LFAB_09310 {ECO:0000313|EMBL:ETY74006.1};
OS Lactiplantibacillus fabifermentans T30PCM01.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=1400520 {ECO:0000313|EMBL:ETY74006.1, ECO:0000313|Proteomes:UP000019247};
RN [1] {ECO:0000313|EMBL:ETY74006.1, ECO:0000313|Proteomes:UP000019247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T30PCM01 {ECO:0000313|EMBL:ETY74006.1,
RC ECO:0000313|Proteomes:UP000019247};
RX PubMed=24558238;
RA Treu L., Vendramin V., Bovo B., Giacomini A., Corich V., Campanaro S.;
RT "Genome Sequence of Lactobacillus fabifermentans Strain T30PCM01, Isolated
RT from Fermenting Grape Marc.";
RL Genome Announc. 2:e00060-e00014(2014).
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:ETY74006.1}.
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DR EMBL; AWWK01000040; ETY74006.1; -; Genomic_DNA.
DR RefSeq; WP_033614110.1; NZ_KK036493.1.
DR AlphaFoldDB; W6T6Y2; -.
DR STRING; 1400520.LFAB_09310; -.
DR PATRIC; fig|1400520.3.peg.1815; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_0_9; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000019247; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; 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; 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 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:ETY74006.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 194..322
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 382..518
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 583 AA; 62164 MW; B2EA66FE6727E84D CRC64;
MTKMTAGRAL AQVLTAWNVD HLYGITADSI NNTVDGLYAE RENLKYIQVR HEEVGALAAA
ADAKLTGKIG VSFGSAGPGA VHLLNGLYDA KMDRVPVLAL VGQSATGVMN TNFFQEMNQD
PMFVDVATFH KQVTNAEQIP YVVDEAIRSA YATHSVSVVI LPDDLSGQEI DFDGFKTANL
THVTTKPVLD AAAVNTVAEQ LAAANQPIMW VGQGARASRE AVVKVAEQFN LPVLSTAPAT
GTMPTDHPLF MGSRGRLGTK PAFEVSQAAD LVLFVGTNFP FARYLPAGVK FIQVNNNLAD
LGKQHDADMT VLADAGDFLT ALAATGVTRP VTNFVTAAKQ DKANWDTWLA KLAADDHDGL
AAEGVMAAIK AASDEDAVFG LDVGNNTEWA IRQLPFNRDQ RFAMSAWYGT MGFGLPAGLA
GKLSNPDKQV WSISGDGGFA MVMPDILTEV KYQLPVVNVV LENKALGFIA HEKIQAGQAP
YGIDLVGADW AGMAENMGAI GLKATNLAEL KVAMAKIKQL QADGNQLPIV LDAKIKNVDP
IDTSFVPVDP DSFDADTIKA YREQYNVSGS DQPALSNLLK DLA
//