ID E0NHE0_PEDAC Unreviewed; 583 AA.
AC E0NHE0;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=Pyruvate oxidase {ECO:0000313|EMBL:EFL95151.1};
DE EC=1.2.3.3 {ECO:0000313|EMBL:EFL95151.1};
GN Name=spxB {ECO:0000313|EMBL:EFL95151.1};
GN ORFNames=HMPREF0623_1463 {ECO:0000313|EMBL:EFL95151.1};
OS Pediococcus acidilactici DSM 20284.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Pediococcus; Pediococcus acidilactici group.
OX NCBI_TaxID=862514 {ECO:0000313|EMBL:EFL95151.1, ECO:0000313|Proteomes:UP000004470};
RN [1] {ECO:0000313|EMBL:EFL95151.1, ECO:0000313|Proteomes:UP000004470}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20284 {ECO:0000313|EMBL:EFL95151.1,
RC ECO:0000313|Proteomes:UP000004470};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
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:EFL95151.1}.
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DR EMBL; AEEG01000007; EFL95151.1; -; Genomic_DNA.
DR RefSeq; WP_004166510.1; NZ_GL397067.1.
DR AlphaFoldDB; E0NHE0; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_0_9; -.
DR Proteomes; UP000004470; Unassembled WGS sequence.
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; 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 Oxidoreductase {ECO:0000313|EMBL:EFL95151.1};
KW Pyruvate {ECO:0000313|EMBL:EFL95151.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004470};
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..321
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 382..517
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 583 AA; 63382 MW; E836E20792513ADC CRC64;
MAKMKAGQAL AQVLKSWDVD HIYGITADSI NNTVDGLYQE RDGLKYIQVR HEEVGSLAAT
ADAKLTGKIG VSFGSAGPGA THMFNGLYDA KMDHAPVLAL IGQSSTEVMN TNFFQEMNQD
PMFVDVAVFH KQVVSAAQIP YVVDEAIRAA YAQKGPAVVI IPDNLSGQEI DYTPIKTPKI
YQQPVHSAID DSAINDTIAA LKAAKHPVLW IGRGVAGARQ QVIQFSEDFQ TPVVTAVPGT
GIMPSDHPSF MGSMGRLGTK PAFEVAQKAD LILFVGTNFP FARFWPDNVK VIQVNNNPED
LGKQRDADMA ILADAKEFLD AILAQNVKLP ASKWLQAAQK DKANWDAWLE KLSKDDHQGL
RAESVMAAIK DHAADNTIFG LDVGNNTEWA IRQIPLNHDQ KFTLSGWFAT MGYGLPAGMA
AKLSYPDRPV VTISGDGGFA MVMQDLLTEV KYEMPIVNVV LENKSFGFIQ HEKLVANQAP
YGIDLQGANW AGVAENMGAI GLTATDLPSL AQAFDKIDEL QKAGNTKPIV LDAKIVNNDP
VDTSFMPLDP QIFDEATIKA FREQYELTDG QPALSEILNE LGE
//
