ID A0A0P6SIK4_9STRE Unreviewed; 580 AA.
AC A0A0P6SIK4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Pyruvate oxidase {ECO:0000313|EMBL:KPJ22081.1};
GN ORFNames=AKK44_06410 {ECO:0000313|EMBL:KPJ22081.1};
OS Streptococcus phocae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=119224 {ECO:0000313|EMBL:KPJ22081.1, ECO:0000313|Proteomes:UP000049578};
RN [1] {ECO:0000313|EMBL:KPJ22081.1, ECO:0000313|Proteomes:UP000049578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51973 {ECO:0000313|EMBL:KPJ22081.1,
RC ECO:0000313|Proteomes:UP000049578};
RA Avendano-Herrera R.;
RT "Genome sequence of Streptococcus phocae subsp. phocae ATCC 51973T isolated
RT from liver specimen obtained from seal.";
RL Submitted (AUG-2015) 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:KPJ22081.1}.
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DR EMBL; LHQM01000029; KPJ22081.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P6SIK4; -.
DR STRING; 119224.AKK44_06410; -.
DR PATRIC; fig|119224.3.peg.1017; -.
DR Proteomes; UP000049578; 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:KPJ22081.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 194..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 580 AA; 63873 MW; C9A7A7F21A73E5A4 CRC64;
MTKINASDAM IKVIEAWGVT NIYGLPGGSF DSTMNALHQR KNTINYIQVR HEEAGALAAV
GEAKVTGRLG VTFGSAGPGA VHLLNGLYDA KHDGVPILAL IGQVPTTNMN KSFFQELNEN
PMFEDVSVYN RTVMTAQQLP YVVDEAIRQA YAHKGVAVVT IPKDLGWQEI EDDYVSTAPH
YQTPLLPEPS DDLIDQALAL LEAAKKPLIY IGLGTKGARE DIMALARQLK APVLSSAPAK
GIVPDDFELY MGSAGRVSTK PGVEMLQEAD TIITFGTDMP FQGFFIKDDA TYIQVDIDGT
KFGRRHRVDL AILADAKKTI KALLEKGREL PESDWYNVAL LNKKNWVEWM ASFEDKEQSP
LRVEPVFKAI NDMATKDAIF QIDVGNVTID ALRYLKMNDQ QAFTTSGWYA TMGYALPAAI
GAQAQYPNRQ VWSISGDGGW TMNMQDIATA VKYQMPIINI ILTNDSLGFI EAEQDDMPQP
HSGIDLIDVD FGRAASAMGA TGFEVRNLDE LKEAFEHAKT ATGPVVIDVK IANDRPIPVE
QLRLDNTRYS QEEVDAFVNT YQADGLIPYS TLLKQVQTRN
//
