ID A0A1E8GL41_9LACT Unreviewed; 616 AA.
AC A0A1E8GL41;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Pyruvate oxidase {ECO:0000313|EMBL:OFI48965.1};
GN ORFNames=BG261_04700 {ECO:0000313|EMBL:OFI48965.1};
OS Floricoccus tropicus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Floricoccus.
OX NCBI_TaxID=1859473 {ECO:0000313|EMBL:OFI48965.1, ECO:0000313|Proteomes:UP000178622};
RN [1] {ECO:0000313|Proteomes:UP000178622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DF1 {ECO:0000313|Proteomes:UP000178622};
RA Chuah L.-O., Yap K.-P., Thong K.L., Liong M.T., Ahmad R., Rusul G.;
RT "Draft genome sequence of a novel species of the family Streptococcaceae
RT isolated from flowers.";
RL Submitted (SEP-2016) 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:OFI48965.1}.
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DR EMBL; MKIR01000022; OFI48965.1; -; Genomic_DNA.
DR RefSeq; WP_070792567.1; NZ_MKIR01000022.1.
DR AlphaFoldDB; A0A1E8GL41; -.
DR STRING; 1859473.BG261_04700; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000178622; 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 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 Pyruvate {ECO:0000313|EMBL:OFI48965.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000178622};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 17..125
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 205..333
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 394..542
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 616 AA; 68052 MW; C08B465579860997 CRC64;
MTNTDTEISK TVPASVAMLR VIESWGVNHI YGYPGGSFNS TMHALDLEKD NIDYIQIRHE
QVGALAAAAD AKLTGKIAVC FGSAGPGATN LLTGLYDAKE DHAPVLALIG QVPSTNMNYN
YFQEFVENPM FADVAVYNRL VMTPESLPYV IDKAIREAYK HNGVAVVVIP NDFGYVQIPD
VPYTSHSNTD NKVVVGPLAT DEEVDQFLAM VKEAKRPVFH VGRGIKNGGD KLVELSKKLQ
IPIVMTGLAK GLIPDSYEGN LGTANRAASK AADEIMAVSD LVITIGADFP FANLVYRTHE
FKFIQIDNDR AQFGRHHFLD LGIWSDATAF VEKAIERSEK VEESPYFKAA VADMANWKEY
LDYLTNRNAE PLEFEAVYKE INRIAEPNAV FSIDVGDNII NSFRHLNITP KNKWVISALF
ASMGSGVPGA IAGQLSYPDR QVFNISGDGA FSMVMQDLIT EKKYKLPIIN VVTSNASLNF
IKSEQDDIPM DYSGIYIEDQ DFAMIAQAMG VESITVRSPK ELPAAFDKAL EVTKAGRPFL
IDAKITDKRS IPVEDLLLKI EDGKLVETVS KNYDASPSTQ TAAGYKEYTV REFLDRYDGQ
NLKPLPELFE EYGVEL
//
