ID A0A0R1ZVK0_9LACO Unreviewed; 590 AA.
AC A0A0R1ZVK0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Pyruvate oxidase {ECO:0000313|EMBL:KRM54844.1};
GN ORFNames=FC18_GL002261 {ECO:0000313|EMBL:KRM54844.1};
OS Lacticaseibacillus sharpeae JCM 1186 = DSM 20505.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1291052 {ECO:0000313|EMBL:KRM54844.1, ECO:0000313|Proteomes:UP000051679};
RN [1] {ECO:0000313|EMBL:KRM54844.1, ECO:0000313|Proteomes:UP000051679}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20505 {ECO:0000313|EMBL:KRM54844.1,
RC ECO:0000313|Proteomes:UP000051679};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRM54844.1}.
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DR EMBL; AYYO01000044; KRM54844.1; -; Genomic_DNA.
DR RefSeq; WP_056976124.1; NZ_AYYO01000044.1.
DR AlphaFoldDB; A0A0R1ZVK0; -.
DR STRING; 1291052.FC18_GL002261; -.
DR PATRIC; fig|1291052.5.peg.2329; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000051679; 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:KRM54844.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051679};
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..322
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 384..531
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 590 AA; 63813 MW; 80313E83AF44BC12 CRC64;
MVKQINAADA MIKVLEDWGI HQIYGIPGGS FDSTMNALHN RRNTMRYIQV RHEEVGALAA
AGEAKITGKI GATFGSAGPG AVHLLNGLYD AKHDHVPVLA LVGQVATSAM NTDYFQEMNE
NPMFADVAVY NRTVMTAQQM PHVVDEAIRQ AYKHSGVAVV TIPTDLGWVA IDDDYVSSAK
LYQRPLLPVP DVGRIDQALA ILGAAKRPVM YVGQGAKDAA DDVLTLSAKL SIPIVVTALG
KDVIPDDYKA NMGSAGRVAT KPGVETARAA DAVLFLGSDF PFQPYFINPD AKYIQVDIDA
SKFGRRHTVD VAILGDAKQV VASMLARSQA KKPTSWYNAA LANKANWAAW IRSFGESAAE
PMRVEPIFKQ INAMATDDAI FQVDVGNVTI DGMRFLDTSK QQRFTTSGWY ATMGYALPAA
IGAQVEFPDR QVWSISGDGG FAMVMQDIIT QVKYKLPIIN VILSNDSLGF IEAEQDDTRQ
PHSGVDLLPG MRYADASAAL GAAGYEVHNL KELKTAFAAA QHRTGPVVIN VHIANTRPLP
VEQLVLDPEV NTQEEVDAFV KQYQAGGLVP LSELLRRAEA GVEPEEHLGD
//
