ID H7FWV6_9LACO Unreviewed; 628 AA.
AC H7FWV6;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Pyruvate oxidase {ECO:0000313|EMBL:EIA33438.1};
GN ORFNames=SMXD51_00364 {ECO:0000313|EMBL:EIA33438.1};
OS Ligilactobacillus salivarius SMXD51.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=1108963 {ECO:0000313|EMBL:EIA33438.1, ECO:0000313|Proteomes:UP000003657};
RN [1] {ECO:0000313|EMBL:EIA33438.1, ECO:0000313|Proteomes:UP000003657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMXD51 {ECO:0000313|EMBL:EIA33438.1,
RC ECO:0000313|Proteomes:UP000003657};
RX PubMed=22582370; DOI=10.1128/JB.00344-12;
RA Kergourlay G., Messaoudi S., Dousset X., Prevost H.;
RT "Genome Sequence of Lactobacillus salivarius SMXD51, a Potential Probiotic
RT Strain Isolated from Chicken Cecum, Showing Anti-Campylobacter Activity.";
RL J. Bacteriol. 194:3008-3009(2012).
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:EIA33438.1}.
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DR EMBL; AICL01000002; EIA33438.1; -; Genomic_DNA.
DR RefSeq; WP_003708937.1; NZ_AICL01000002.1.
DR AlphaFoldDB; H7FWV6; -.
DR PATRIC; fig|1108963.3.peg.1820; -.
DR HOGENOM; CLU_013748_3_0_9; -.
DR Proteomes; UP000003657; 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:EIA33438.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 6..116
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"
FT REGION 604..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 628 AA; 69555 MW; D2DBC7D375DB6CD0 CRC64;
MPNKISGADA MLKVLHEWGV THIYGHPGGS LDSTMNALHN QQDKIKFIQV RHEEAGALAA
SASAKLSGKV GVVLGSAGPG AIHLLNGLHD AKADHVPIFA IIAQVPTTKM NIDFFQAYNE
GPWFDNVACW NRTAMTAESI PKLVDEGIRQ AYKHRGVATL ILPKDLGWKM IPDTFVSNAA
NHVEPIYPEP NPQSITDALE LIKAAKAPMV YFGIGAKHAA KELKEISAKF KLPLVSSVLA
KGIIEDTYPT YMGSTGRVAP KTGVELGFNT DLILWIGNDV PFSIFLFNPK AKVIQIDIDS
EKLGKRHQVT VPILADSKKT LQALLKQGEE LPETPFYKAA LANKENWLAW LNRFKHSEDI
PLRPEPVFEV LNQEASDQAI FTLDVGNVNI NFARLMNLHD QQKWTTSGQF ATMGYGVPAA
IAAKILYPDR DVYSLNGDGG FAMLMEEIIT QVKYNLNIIN IIFNNKTLGY IEAEQIDDTQ
QPVFGVDLPD TDWATIAKGM GAIGYTVYTL DDFKEAIAAG KESSKPIVID VKFTREMPFT
TEHMYLDPSY QDPQKVASFI EKYQATTLRP FSYFLKRELG ESRDDFNSAM QNVFDVITTP
STLPENYNQK KKEQDQIIPD AVSGASEY
//
