ID A0A261G4D1_9BIFI Unreviewed; 615 AA.
AC A0A261G4D1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Pyruvate oxidase {ECO:0000313|EMBL:OZG66065.1};
GN ORFNames=BAQU_1399 {ECO:0000313|EMBL:OZG66065.1};
OS Bifidobacterium aquikefiri.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1653207 {ECO:0000313|EMBL:OZG66065.1, ECO:0000313|Proteomes:UP000216451};
RN [1] {ECO:0000313|EMBL:OZG66065.1, ECO:0000313|Proteomes:UP000216451}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 28769 {ECO:0000313|EMBL:OZG66065.1,
RC ECO:0000313|Proteomes:UP000216451};
RX PubMed=28764658; DOI=10.1186/s12864-017-3955-4;
RA Lugli G.A., Milani C., Turroni F., Duranti S., Mancabelli L.,
RA Mangifesta M., Ferrario C., Modesto M., Mattarelli P., Jiri K.,
RA van Sinderen D., Ventura M.;
RT "Comparative genomic and phylogenomic analyses of the Bifidobacteriaceae
RT family.";
RL BMC Genomics 18:568-568(2017).
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:OZG66065.1}.
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DR EMBL; MWXA01000006; OZG66065.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261G4D1; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000216451; 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:OZG66065.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000216451};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 24..138
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 215..344
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 405..553
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 615 AA; 68307 MW; A887F1FE704EA5BB CRC64;
MAKNVIQFGF DTKVANRHEV GTIKAGVAVV KLLESWGVKH IYGIPGGSIN SLMDALYEEK
QNIDYIQVRH EEVGAMAAAM HAKMTGEIGV CFGSAGPGGT HLMNGLYDAR EDHVPVLALV
GQFGTAGMNW DTFQEINENP IFADVAIYNR TVMTADQLPH VVDEAIRQAY AKNGVAVVQI
PVNLGWVNID TDAWYSAAHA HRRYPNPTLD PEDIALAVNI LNEAERPVIF AGIGTRGKSK
IVIDLCRKIK APLANTGISW DNFPSDFEAL LGSPNRVSTK PSVEVFPEAD VVVFVGNNYP
FAEVSKIFKN VKKFIQIDID PSKLGKRHYT DVAILGDAGD ALKAIYEKVD EKPDNGWWRA
NLDNVVNWNE YVHRLETKTE GELQLYQVYN QINRVSEKDA IYSIDVGDVT QTSIRHLHMN
PQQMWRTSAL FATMGIGLPG AIAAKLDFPG RQVWNLAGDG GFNMVMQDLA TQVQYKLPII
NVVFANQQYG FIKDEQEDTN KGFLGVQFQD TDYKKLAESM GAVGYSVTKI SQLEDVFDAA
IRDIANGRVV VIDAKISNER PLPAELLELD PRLSSDEDIE RFKQRYEAED LKPLSYFLEK
EGLESHIGKI EQGGF
//
