ID Q04FC3_OENOB Unreviewed; 586 AA.
AC Q04FC3;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 24-JAN-2024, entry version 92.
DE SubName: Full=Pyruvate oxidase {ECO:0000313|EMBL:ABJ56849.1};
DE EC=1.2.3.3 {ECO:0000313|EMBL:ABJ56849.1};
GN OrderedLocusNames=OEOE_0936 {ECO:0000313|EMBL:ABJ56849.1};
OS Oenococcus oeni (strain ATCC BAA-331 / PSU-1).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Oenococcus.
OX NCBI_TaxID=203123 {ECO:0000313|EMBL:ABJ56849.1, ECO:0000313|Proteomes:UP000000774};
RN [1] {ECO:0000313|EMBL:ABJ56849.1, ECO:0000313|Proteomes:UP000000774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-331 / PSU-1 {ECO:0000313|Proteomes:UP000000774};
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M., Klaenhammer T., Richardson P.,
RA Kozyavkin S., Weimer B., Mills D.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP000411; ABJ56849.1; -; Genomic_DNA.
DR RefSeq; WP_002821800.1; NC_008528.1.
DR AlphaFoldDB; Q04FC3; -.
DR STRING; 203123.OEOE_0936; -.
DR KEGG; ooe:OEOE_0936; -.
DR PATRIC; fig|203123.7.peg.949; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_0_9; -.
DR OMA; IGVKFGC; -.
DR Proteomes; UP000000774; Chromosome.
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; 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 Oxidoreductase {ECO:0000313|EMBL:ABJ56849.1};
KW Pyruvate {ECO:0000313|EMBL:ABJ56849.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000774};
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..322
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 382..532
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 586 AA; 63942 MW; 03220983CDE7D913 CRC64;
MTKMIAGRAL VKALEDWGVD HVYGIPGGSI NHTVEGLYLE QDKVKYIQVR HEEVGALAAS
ADAKFTGKIG VAFGSAGPGA THLFNGLYDA KMDHVPLLAI IGQVPQETMN TNYFQEMDEV
PLFSDVSVYN RTVTTAEQIP YVINQAIREA YRQKGVATVV LPENLAAKEI DYKETKTPKV
VANNFSQKVD SKAVSDTLAM LKAAKHPLIY AGRGLLGARD VLTKFSEQFN IPVMNTVPAT
GVISTDDPNF IGTFGRLGSK SGFEALQHTD LILFLASEFP FAGFWPKNIK VIEVNNNPFD
IGKTVDVDYA VISDAKSYLQ ALINTGQTLP AGNWLKANQE NKRNWDNWLA ELAKDESDGL
NPESVTAKIA SMVGPNDTYA VDTGNVSEWG ARGLPMNHNQ RFAISGLFAT MGFGLPGGLA
GALSVPDGQA WSLSGDGGFS MVVQDLITEV RYGLPVINIV FSNDRFGFIY HEQVQTKQHF
YGVDLTGADW AKVSEGLGAI SFTVKTIADI DQVFTKIKKL QESGNKKPIV VNAVIKKDDP
FPTDYMPLDP KLYGQDAVDQ YAEKYHFDLE KQPSLGALLR AQGDNL
//