ID A0A261G6H0_9BIFI Unreviewed; 579 AA.
AC A0A261G6H0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Pyruvate oxidase {ECO:0000313|EMBL:OZG67020.1};
GN ORFNames=BAQU_1092 {ECO:0000313|EMBL:OZG67020.1};
OS Bifidobacterium aquikefiri.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1653207 {ECO:0000313|EMBL:OZG67020.1, ECO:0000313|Proteomes:UP000216451};
RN [1] {ECO:0000313|EMBL:OZG67020.1, ECO:0000313|Proteomes:UP000216451}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 28769 {ECO:0000313|EMBL:OZG67020.1,
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:OZG67020.1}.
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DR EMBL; MWXA01000005; OZG67020.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261G6H0; -.
DR Proteomes; UP000216451; 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:OZG67020.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000216451};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 6..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 195..324
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 384..531
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 579 AA; 62852 MW; 1E84CF3F3AD55CE0 CRC64;
MFMSTKAADQ LVSVLMNWKV KHVFGLPGDS IDTTVDALRR NQEKIKFVQV RHEEVAALSA
AANAKLTGGV GVCLAIGGPG AIHLLNGLYD AKMDHVPVLA LLGQVTTKDI NEGYFQEVNT
PKLFDDVAVF NKTISASDNL GKVVDSAIRA AMTKKGVAVL TIPDDLPDHK VTNEYKDSAA
AFKLSTPQVD DEQLAEAISM VQQAQKPLAL IGKGGEHAGA ELQKFVETNN IPFILTMPAK
GTIADDHANS LGNVGKLGTK PAYEAMKSTD LLLMIGTNYP YTPYLPDAGQ AKCIQIDTCP
ENLGSRYAVD LAIDGDAGAV VSQLNAKGAL RSDDRFLKAC QKDMDIWNKW MSEKRSLNTT
PASPEAVFAS IDETAPKDAV YSIDVGTSTS WGARFLHVQP TQKYSISAWL GTMGCGLPSA
IAGAESYPER KNISVSGDGA FAMVMQDFVT AVKYKLPIIQ VVINNQKLAF IEYEQQSAGQ
LNYEIDLEDM DYAKFAEAAG GVGYTARSNA EFKDALEKAY KETDKPVLIN VYVKDNAPLP
GKIVGEEAMG YTKYGTHYLE NYWKIPSMPP LKDIMRQFF
//
