ID R3U700_9ENTE Unreviewed; 575 AA.
AC R3U700;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Pyruvate oxidase {ECO:0000313|EMBL:EOL49228.1};
GN ORFNames=UC3_00131 {ECO:0000313|EMBL:EOL49228.1};
OS Enterococcus phoeniculicola ATCC BAA-412.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1158610 {ECO:0000313|EMBL:EOL49228.1, ECO:0000313|Proteomes:UP000013785};
RN [1] {ECO:0000313|EMBL:EOL49228.1, ECO:0000313|Proteomes:UP000013785}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-412 {ECO:0000313|EMBL:EOL49228.1,
RC ECO:0000313|Proteomes:UP000013785};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Enterococcus phoeniculicola BAA-412.";
RL Submitted (FEB-2013) 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:EOL49228.1}.
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DR EMBL; AJAT01000005; EOL49228.1; -; Genomic_DNA.
DR RefSeq; WP_010766818.1; NZ_KB946325.1.
DR AlphaFoldDB; R3U700; -.
DR STRING; 154621.RV11_GL002303; -.
DR PATRIC; fig|1158610.3.peg.107; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_0_9; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000013785; 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; 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 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:EOL49228.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000013785};
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..323
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 383..529
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 575 AA; 63228 MW; 05C12AD7CFE6D078 CRC64;
MSNKINAGIA MIKVFESWGV DHIYGIPGGS FNSTMDALYH ERESVKYIQV RHEEVGALAA
AADAKLTGKV GVVFGSAGPG ASHLINGLYD AQMDHVPVVA LLGQVASTAM NYNSFQELNE
NPMFADVSVY NRTVMTPESL PHVVDEAIKA AYEHNGVAVV TIPVDFGFKE IDDTFVSTAH
NHRTGVILPQ EDQLNEALPL IKEAKQPILY IGQGTRGGWE AIKAFSEHFS MPVAAAVLAK
GIVPDSYENF LGFAARVATK PANEALAVAD LIVFVGSDFP FARYFFNPKA KFIQIDIDAT
KFGRRHKTDV SILGDGATAL RKLVELGTQR PKDEWLLANQ ENKRNWVNWL ASFSDSKDEP
LRPEPVYAQI NRIAEKDAIF VTDVGNTTIH SIRLLDLNGQ QKHTTSGWFA TMGNGVPGGI
AAQLSYPDRQ VFTLSGDGAF AMVMQDIITQ VKYNLPIINV VFSNESFGFI EAEQEDTEQK
KFGVFLEGAD FGKVGEALGA VGFTITRYDQ LQPAFEAAKN SKRPVVIDIK IKNQRPLPVE
ELVLDPDKFS EQEINAFKEK YDVHDMPALS ELLKK
//