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Database: UniProt
Entry: X0PAM8_9LACO
LinkDB: X0PAM8_9LACO
Original site: X0PAM8_9LACO 
ID   X0PAM8_9LACO            Unreviewed;       434 AA.
AC   X0PAM8;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Pyruvate oxidase {ECO:0000313|EMBL:GAF36483.1};
GN   ORFNames=JCM14108_1452 {ECO:0000313|EMBL:GAF36483.1};
OS   Lentilactobacillus farraginis DSM 18382 = JCM 14108.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lentilactobacillus.
OX   NCBI_TaxID=1423743 {ECO:0000313|EMBL:GAF36483.1, ECO:0000313|Proteomes:UP000019488};
RN   [1] {ECO:0000313|EMBL:GAF36483.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 14108 {ECO:0000313|EMBL:GAF36483.1};
RA   Yuki M., Oshima K., Suda W., Kitahara M., Kitamura K., Iida T., Hattori M.,
RA   Ohkuma M.;
RT   "Draft Genome Sequences of Two Lactobacillus Strains, L. farraginis JCM
RT   14108T and L. composti JCM 14202T, Isolated from Compost of Distilled
RT   Shochu Residue.";
RL   Genome Announc. 2:e00257-14(2014).
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:GAF36483.1}.
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DR   EMBL; BAKI01000012; GAF36483.1; -; Genomic_DNA.
DR   AlphaFoldDB; X0PAM8; -.
DR   STRING; 1423743.FD41_GL000577; -.
DR   Proteomes; UP000019488; 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; 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; IPR011766; TPP_enzyme_TPP-bd.
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.
PE   3: Inferred from homology;
KW   Pyruvate {ECO:0000313|EMBL:GAF36483.1};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          6..121
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..426
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   434 AA;  47251 MW;  625927EC1A3D06B0 CRC64;
     MVEKISGSDA VLKVLEQWGV TNIYGLPGGS FDSTMNAIHN QKNKINFIQV RHEEAGAIAA
     SASAKLTGKV GVCFGSAGPG AVHLLNGLYD AKSDGVPVVA LVAQVPTSNM NMDFFQAMDE
     EPIFDDVAVW NRTAMTAEAL PRMTDEAIRQ AYMKHGVAVL TIPKDLGWAQ INDTYEPNVN
     SHTEPAYPDP RPEDVTEAVK LIKEAKSPMI YFGLGAKDAA DELKAASEKF KMPLVSSVLA
     KGIIDDNYPA YLGSTGRVAP KPGAEIGFST DLILWVGNDV PFSIFLFNKK AKVIQIDIES
     EKLGKRRHND VSMLADSKKA LQAILDAGEE RKPSAFYQAA LADKTNWLDW QNSFKDSTEK
     PVRPEPIFDV INQTASDKAI FAVDVGNVNI NFERLIDMHG DQKWATSGIY ATMGFALPTS
     IAAKLEYLTV TFTA
//
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