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Database: UniProt
Entry: F9UM63_LACPL
LinkDB: F9UM63_LACPL
Original site: F9UM63_LACPL 
ID   F9UM63_LACPL            Unreviewed;       579 AA.
AC   F9UM63;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   SubName: Full=Pyruvate oxidase {ECO:0000313|EMBL:CCC78302.1};
DE            EC=1.2.3.3 {ECO:0000313|EMBL:CCC78302.1};
GN   Name=pox1 {ECO:0000313|EMBL:CCC78302.1};
GN   OrderedLocusNames=lp_0849 {ECO:0000313|EMBL:CCC78302.1};
OS   Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS   (Lactobacillus plantarum).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=220668 {ECO:0000313|EMBL:CCC78302.1, ECO:0000313|Proteomes:UP000000432};
RN   [1] {ECO:0000313|EMBL:CCC78302.1, ECO:0000313|Proteomes:UP000000432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1
RC   {ECO:0000313|Proteomes:UP000000432};
RX   PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA   Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA   Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W., Stiekema W.,
RA   Lankhorst R.M., Bron P.A., Hoffer S.M., Groot M.N., Kerkhoven R.,
RA   de Vries M., Ursing B., de Vos W.M., Siezen R.J.;
RT   "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=WCFS1;
RA   Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA   Kleerebezem M., van Hijum S.A.F.T.;
RT   "Complete resequencing and reannotation of the Lactobacillus plantarum
RT   WCFS1 genome.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:CCC78302.1, ECO:0000313|Proteomes:UP000000432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1
RC   {ECO:0000313|Proteomes:UP000000432};
RX   PubMed=22156394; DOI=10.1128/JB.06275-11;
RA   Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA   Kleerebezem M., van Hijum S.A.F.T.;
RT   "Complete resequencing and reannotation of the Lactobacillus plantarum
RT   WCFS1 genome.";
RL   J. Bacteriol. 194:195-196(2012).
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; AL935263; CCC78302.1; -; Genomic_DNA.
DR   RefSeq; WP_011101179.1; NC_004567.2.
DR   RefSeq; YP_004888816.1; NC_004567.2.
DR   AlphaFoldDB; F9UM63; -.
DR   SMR; F9UM63; -.
DR   STRING; 220668.lp_0849; -.
DR   EnsemblBacteria; CCC78302; CCC78302; lp_0849.
DR   GeneID; 77217366; -.
DR   KEGG; lpl:lp_0849; -.
DR   PATRIC; fig|220668.9.peg.722; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_3_0_9; -.
DR   OMA; TLMGWGA; -.
DR   OrthoDB; 4494979at2; -.
DR   PhylomeDB; F9UM63; -.
DR   Proteomes; UP000000432; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0047112; F:pyruvate oxidase activity; IEA:UniProtKB-EC.
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   Oxidoreductase {ECO:0000313|EMBL:CCC78302.1};
KW   Pyruvate {ECO:0000313|EMBL:CCC78302.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000432};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          5..118
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          193..321
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          382..529
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   579 AA;  63498 MW;  A8D3E53A0E0D7534 CRC64;
     MAKISGSDAV LKVIQKWGVK HIYGLPGGSF DSTMNAIYNQ RKTLKYIQVR HEEAGAIAAS
     ADYKLTGKIG VCFGSAGPGA VHLLNGLYDA KEDGIPMLAI VAQVPTKRMN MDFFQAMNEE
     PIFDDVAVWN RTAMTAESLP MMTDEAIRQA YAHNGVAVLT IPKDFGWAEI EDNFETNASV
     HTVNYPAPTA ESVADAVKLI KAAKSPMIYF GVGAKDAAEE LKAASEKFKM PLVSSVLAKG
     IIEDDYPAYL GSTGRVAPKP GAEIGFSTDL ILWVGNNVPF SIFLFNKKAK VIQIDIDSEK
     FGKRHHTNVA IQADAKKALA AINAAGEARD DSAFYDAAVA DKKNWDKWQA SFNDSTESPV
     RPEPIFDVLN QEASDKAVWA IDVGNVNINF ERLIRMHDDQ KWATSGIYAT MGFGVPAALA
     AKVNYPDRDV YSLSGDGAFA MLSEEILAQV KYNLHIINIV FSNETLGFIE AEQTDDSHQP
     LSGVDLPDTD WAKVGEGYGA VGYTVRTKAE FKQALEDAKK TDKPVVIDVK LTHAMPFTTE
     HMYLDDAWQD KDKIAEFVKK YDAQALKPFS YFLKQAQTN
//
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