ID A9IMK2_BORPD Unreviewed; 589 AA.
AC A9IMK2;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Pyruvate oxidase {ECO:0000313|EMBL:CAP42719.1};
DE EC=1.2.3.3 {ECO:0000313|EMBL:CAP42719.1};
GN OrderedLocusNames=Bpet2376 {ECO:0000313|EMBL:CAP42719.1};
OS Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=340100 {ECO:0000313|EMBL:CAP42719.1, ECO:0000313|Proteomes:UP000001225};
RN [1] {ECO:0000313|EMBL:CAP42719.1, ECO:0000313|Proteomes:UP000001225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448
RC {ECO:0000313|Proteomes:UP000001225};
RX PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA Gross R., Guzman C.A., Sebaihia M., Martins Dos Santos V.A., Pieper D.H.,
RA Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA Schneiker-Bekel S., Schulze K., Vorhoelter F.J., Yevsa T., Engle J.T.,
RA Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA Martinez-Arias R.;
RT "The missing link: Bordetella petrii is endowed with both the metabolic
RT versatility of environmental bacteria and virulence traits of pathogenic
RT Bordetellae.";
RL BMC Genomics 9:449-449(2008).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; AM902716; CAP42719.1; -; Genomic_DNA.
DR AlphaFoldDB; A9IMK2; -.
DR STRING; 94624.Bpet2376; -.
DR KEGG; bpt:Bpet2376; -.
DR eggNOG; COG0028; Bacteria.
DR Proteomes; UP000001225; 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:CAP42719.1};
KW Pyruvate {ECO:0000313|EMBL:CAP42719.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 199..328
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 388..542
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 589 AA; 63819 MW; 4732F15D2A1CA01E CRC64;
MQTVSDFVLS RLAQWGIQRV YGYPGDGING LIGAFGRTRE PLEFVQARHE EMAAFMACAH
AKFTGQVGVC MATSGPGAIH LLNGLYDAKL DHQPVVAIVG QQARSALGGD YQQEVDLVSL
FKDVAHDFVH SAVSPVQVRH LVDRAIRIAM ERRAVTCLIL PNDVQDLPAV PAPPREHGTV
HTGIGVTSHA GVPAPTALQN AADILNKGER VAILAGAGAR DAGEELLQVA ELLGAGVAKA
LLGKCVVPDD VPYVTGSIGL LGTQPSWRMM NDCDTLLMVG TAFPYGEFLP PEGQARAVQI
DRDGRMISLR YPVEQGLVGD SKATLRALAP LLQPKQSRRW RDKIEKDVAQ WWQTVEARAM
VAARPLNPQR PFWELSPRLP DRSIITCDSG SAASWYAQQL RLRKGMTASL SGGLASMGSG
VPYALAAKLA HPDRPVFALV GDGALQMNGM NELITVAHRW RDWADPTLVV MVLNNGDLNM
VTWEQRVMGG DPRFKDSQLL PPFPYAEYAE LLGLEGIRVD DPDQVGPAWD RAIAAGRPVL
IEMVTDPEVP PIPPHVPLKQ VQNYVKALRQ EDASGGAALR ATIKQWWAG
//
