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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//