GenomeNet

Database: UniProt
Entry: A0A0R2A2E9_9LACO
LinkDB: A0A0R2A2E9_9LACO
Original site: A0A0R2A2E9_9LACO 
ID   A0A0R2A2E9_9LACO        Unreviewed;       590 AA.
AC   A0A0R2A2E9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Pyruvate oxidase {ECO:0000313|EMBL:KRM61120.1};
GN   ORFNames=FC26_GL002338 {ECO:0000313|EMBL:KRM61120.1};
OS   Paucilactobacillus vaccinostercus DSM 20634.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Paucilactobacillus.
OX   NCBI_TaxID=1423813 {ECO:0000313|EMBL:KRM61120.1, ECO:0000313|Proteomes:UP000051733};
RN   [1] {ECO:0000313|EMBL:KRM61120.1, ECO:0000313|Proteomes:UP000051733}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20634 {ECO:0000313|EMBL:KRM61120.1,
RC   ECO:0000313|Proteomes:UP000051733};
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:KRM61120.1}.
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; AYYY01000043; KRM61120.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R2A2E9; -.
DR   STRING; 1423813.FC26_GL002338; -.
DR   PATRIC; fig|1423813.3.peg.2385; -.
DR   Proteomes; UP000051733; 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:KRM61120.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051733};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          15..129
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          205..333
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          394..540
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   590 AA;  64011 MW;  5F83512CE12795D2 CRC64;
     MIVFLEEDVK MSKINAADAM IKVLEDWHVD HLFGLPGGSF DSTMNALHNR KSTMKYIQVR
     HEETGAIAAA GEAKLTGKIG VTFGSAGPGA VHLLNGLYDA KHDHAPVLAL VAQVPTSAMN
     TDFFQELNEN PIFADVSVYN RTVMTAEQLP AVVDQAIRQA YEHSGVAVVT IPKDLGWAEI
     EDNYVSTADN YVVTDNYPLP DQTAVDKAVE ILTNAKRPLI YFGLGAKKAA KELKQLSDQL
     KIPLMSSALA KGVITDADEA YMGSAGRVAT KPGVDAASNA DAILFVGSNF PFASFFFNPA
     AKFIQVDVKP TNIGKRHHVD VGLLADAKTA LQAFIDRSSA VESRAYYDAL VADKKNWLEW
     LKKFVNEDQT PLRVDTVFEQ INQIAKDDAV FALDVGNVTI DGVRLLKMKP TQKITTSGWY
     ATMGYALPTA IAAQASYPDR QVFSISGDGG FTMVMHDILT QVKYRQPIIN VVLTNESLGF
     IEAEQDDTGQ PHSGVDLIDA NFGDAATALG AKGYEVKTLA ELKAAFKDAQ TVNGPTVIDV
     KISDDRPLPV EQLVLEADGN HTQADVDAFV KQYHADGLIP FSQLLNQFNA
//
DBGET integrated database retrieval system