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
//