ID A0A3E0H7F8_9PSEU Unreviewed; 597 AA.
AC A0A3E0H7F8;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Pyruvate dehydrogenase (Quinone) {ECO:0000313|EMBL:REH39382.1};
GN ORFNames=BCF44_113237 {ECO:0000313|EMBL:REH39382.1};
OS Kutzneria buriramensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kutzneria.
OX NCBI_TaxID=1045776 {ECO:0000313|EMBL:REH39382.1, ECO:0000313|Proteomes:UP000256269};
RN [1] {ECO:0000313|EMBL:REH39382.1, ECO:0000313|Proteomes:UP000256269}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45791 {ECO:0000313|EMBL:REH39382.1,
RC ECO:0000313|Proteomes:UP000256269};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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:REH39382.1}.
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DR EMBL; QUNO01000013; REH39382.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E0H7F8; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000256269; 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:REH39382.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 199..329
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 389..544
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 171..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 597 AA; 64378 MW; 8C81B79DC534A5C5 CRC64;
MAETVGDYLL GRLRDWQVDQ VFAYPGDGIN GIVAAFGRAD DTPRFIQARH EEMAAFEAVG
YAKFSGKVGI CMATSGPGAI HLLNGLYDAK LDHVPVVAIV GQTARSAMGA SYQQEVDLQS
LFKDVASAYL VEVNVPEQLP NALDRAIRVA EAERTPTAVI IPSDLQEQPY SPPQHVFKQS
PSSPPSHPHT VTVPDLAEIE RAADVINAGS KVAILCGQGA RAAADEVRQL AELTGAGVAK
ALLGKDVLPD DLSYVTGSIG LLGTRPSYEL MTGCDTLVII GSNFPYSQFL PEYGKARAIQ
IDIDGKFIGM RYPTEVNLVA DAKATLAALL PKIERKGDRS WRETIESNVA KWWETMERES
MVDADPVNPM RITWELSACI PDNAIVTSDS GSAANWYART LKMRAGMRGS LSGTLATMGP
GVPYAIGAKF AHPDRPAIAL VGDGAMQMNG LAELITIKRY YERWSDPRCV ICVLHNNDLN
QVTWELRAMG GAPKFEESQV LPDIDYAAIA RSFGLGGIVV TEPDRLGAAW EEAFAADRPV
VLDVHCDPNV PPIPPHATFE QVKAAAESVL KGDPDAFGLV TQGIKTKLQE FVPGSRK
//