ID A0A0R2ER44_9LACO Unreviewed; 581 AA.
AC A0A0R2ER44;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Pyruvate oxidase {ECO:0000313|EMBL:KRN17830.1};
GN ORFNames=FD14_GL002555 {ECO:0000313|EMBL:KRN17830.1};
OS Secundilactobacillus similis DSM 23365 = JCM 2765.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Secundilactobacillus.
OX NCBI_TaxID=1423804 {ECO:0000313|EMBL:KRN17830.1, ECO:0000313|Proteomes:UP000051442};
RN [1] {ECO:0000313|EMBL:KRN17830.1, ECO:0000313|Proteomes:UP000051442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23365 {ECO:0000313|EMBL:KRN17830.1,
RC ECO:0000313|Proteomes:UP000051442};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRN17830.1}.
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DR EMBL; AYZM01000171; KRN17830.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2ER44; -.
DR STRING; 1423804.FD14_GL002555; -.
DR PATRIC; fig|1423804.4.peg.2764; -.
DR Proteomes; UP000051442; 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 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 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:KRN17830.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051442};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 193..321
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 382..531
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 581 AA; 63425 MW; C9163EAC1941C8E5 CRC64;
MINAGVAALR TLESWGVTHI YGIPGGTINN LMYALHAERE RIRYIHVRHE EVGALAAVAD
TKLTGHIGVA FGSAGPGATH LYQGAYDAMA DKVPALFIVG QNPQALMNQD FFQEFDETPM
FKDPGVYART VTTAASLPHV LDEAIRRAFA MHGPAIVTIP NDLAGQAIPA DGYYSSAANF
ARPVLAAGKP EQVEEALVLL SKAKKPLLYV GQGTIGAAEE VMRFAQQFQV PVITTALGKE
IIPYEFESLL GSAARVASKP ANEALKETDL MLFIGSNYPF AEEMFKPDVK FIQVDSNPQM
LGKRHRTDVA ILGDAKQTLQ QFLALGTPAS PSAWYAANVD NVRNWHEYND DMMNRTTGEL
RFEPAFKAIN EIAENDAIFS IDVGDVTQNA VRLLKVNGKQ PWITSGLFAT MGVGLPGAIA
AKLDYPGRQV FNLTGDGAAA MVMQDLSTQV TYMLPVINVV FSNQALGFIE DEQEDDGQEW
FGISLPRTDF AKVAEAQGMM GITVRTIDDV KPAFDRAVDL TRAGKPVLID IKMTNERPIP
VEKLALDPAE NDAQTIAAFK KRYYAEKLVP LSQFMHNHHV N
//
