ID A0A0R2CLY9_9LACO Unreviewed; 584 AA.
AC A0A0R2CLY9;
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:KRM89577.1};
GN ORFNames=FD21_GL001085 {ECO:0000313|EMBL:KRM89577.1};
OS Liquorilactobacillus vini DSM 20605.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Liquorilactobacillus.
OX NCBI_TaxID=1133569 {ECO:0000313|EMBL:KRM89577.1, ECO:0000313|Proteomes:UP000051576};
RN [1] {ECO:0000313|EMBL:KRM89577.1, ECO:0000313|Proteomes:UP000051576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20605 {ECO:0000313|EMBL:KRM89577.1,
RC ECO:0000313|Proteomes:UP000051576};
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:KRM89577.1}.
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DR EMBL; AYYX01000003; KRM89577.1; -; Genomic_DNA.
DR RefSeq; WP_010580478.1; NZ_AYYX01000003.1.
DR AlphaFoldDB; A0A0R2CLY9; -.
DR STRING; 1133569.FD21_GL001085; -.
DR PATRIC; fig|1133569.4.peg.1215; -.
DR eggNOG; COG0028; Bacteria.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000051576; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; 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; 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; 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 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:KRM89577.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051576};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 196..322
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 382..517
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 584 AA; 63462 MW; 3D777233E75AB2B7 CRC64;
MTKIKAGQAL AKVLVDWKID HLYGITADSI NNTVDGLYQE RENLKYIQVR HEEIGALAAA
ADAKLTGTIG VSFGSAGPGA VHLLNGLYDA KMDHVPVLAI VGQSATAIMN TNFFQEMNQD
PIFADVAEFH KQVTNAEQIP YVVDEAIRSA YATHSVSVVI IPDDLSGQEI EFNNFKTASI
KAIKQAIAPK AEDLHAVEQA LKAAKQPILW VGKGAFNARQ EVVAVAEKFS LPVLSTAPAT
GVMPTDHPSF MGSRGRLGTK PAFEVSQAAD LVLFVGTNFP FARYLPADIK FVQVNNNLAD
LGKQRDADLT VLSDAKLFLQ ALLKLDYSVA PTPFLKAAQA DKHNWDKWLQ ALAQDDHAGL
RAESVMAAIK KNAAADAVFG LDVGNNTEWA IRQLPLNQQQ RFSMSAWYGT MGFGLPAGLA
GKLSFPDKQN WTISGDGGFA MVMPDLLTEV KYQLPVINIV LENQVFGFIQ HEKLLAHQAP
YGIDLQGADW AKAAEGLGAI GLRATNLAEL KTAMQKINQL QAADNRLPIV LAAKIKNVDP
IDTSFVPVER AIFGDQMVDQ YRQQYAIAED QQPAFSQLLA KFNA
//
