ID A0A286DW94_9ACTN Unreviewed; 603 AA.
AC A0A286DW94;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Pyruvate dehydrogenase (Quinone) {ECO:0000313|EMBL:SOD62932.1};
GN ORFNames=SAMN06297387_10895 {ECO:0000313|EMBL:SOD62932.1};
OS Streptomyces zhaozhouensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1300267 {ECO:0000313|EMBL:SOD62932.1, ECO:0000313|Proteomes:UP000219072};
RN [1] {ECO:0000313|EMBL:SOD62932.1, ECO:0000313|Proteomes:UP000219072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.7095 {ECO:0000313|EMBL:SOD62932.1,
RC ECO:0000313|Proteomes:UP000219072};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; OCNE01000008; SOD62932.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A286DW94; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000219072; 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:SOD62932.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000219072};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 198..328
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 554..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 603 AA; 65134 MW; 04C7E6F48A701C79 CRC64;
MTEKVADHVL DRLREWGVSH VFGYPGDGIN GLLAAWERAG DRPRFLQARH EEMAAFQAVG
YAKFSGGVGV CAATSGPGAV HLLNGLYDAK LDHVPVVALV GQTARSAMGG SYQQEIDLHT
LFKDVASAYL EVVNVPEQLP NVLDRALRTA RALRAPTAVI IPADVQDLDY TPPGHAFKMV
PSSIGASGWT ATPDEAALDR AAEVLNAGEK VAMLVGQGAA GAADEVVETA RVLQAGIAKA
LLGKDVLPDT LPGVTGGIGL LGTRPSYELM RDCDTLLTVG SSLPYSQFLP EYDQARAVQI
DLDPHQIGMR YPYEVNLVGD ARDTLRRLLP RLRPSENGER WRTSMEKAVE RWYDVLARRA
EVEADPVNPE YVAHCLDRLV PENAVLTADS GSVANWYARH VRMRGRMRGS LSGTLASMGC
AVPYAIAAKF AMPDRPAIAL VGDGAMQMNG LAELVTAARY RHEWSDPRLV VAVWNNRDLN
QVSWELRAMG GAPRFEASQS LPDVRYADFA RSLGLEGIRV EKPADVEDGW RRALAADGPA
VVEFLTDPSV PPIPPHASWE QASATAKSLA RGDGDRGAVL RQGVKAKLQD YLPGRRHRDG
GDG
//