ID A0A1I1F924_9ACTN Unreviewed; 600 AA.
AC A0A1I1F924;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Pyruvate dehydrogenase (Quinone) {ECO:0000313|EMBL:SFB95791.1};
GN ORFNames=SAMN05421773_101644 {ECO:0000313|EMBL:SFB95791.1};
OS Streptomyces aidingensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=910347 {ECO:0000313|EMBL:SFB95791.1, ECO:0000313|Proteomes:UP000199207};
RN [1] {ECO:0000313|EMBL:SFB95791.1, ECO:0000313|Proteomes:UP000199207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5739 {ECO:0000313|EMBL:SFB95791.1,
RC ECO:0000313|Proteomes:UP000199207};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; FOLM01000001; SFB95791.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1F924; -.
DR STRING; 910347.SAMN05421773_101644; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000199207; 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:SFB95791.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199207};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..115
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 198..327
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 388..544
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 600 AA; 65634 MW; C06BD236716C48DB CRC64;
MSQVADFVLD RLRQWGVHRV FGYPGDGING FLGAFGRAAG DPEFIQVRHE EMAAFMACGH
AKFTGEPGVC IATSGPGAIH LLNGLYDAKL DHQPVVAVVG QQKRLCLGSA YQQEVHLDRL
FADVSDYCQL VMHPAQARHV VDRAFKNALT NRSVSTIIVP EDVQEEPAQP SPPRMHGAVY
SSVGWSRPRV LPDEDELRRA ARVLNEGKKV AILIGQGAAD AEGEVIETAE TLGAGVAKAL
LGRDVLPDDL PYVTGPVGLL GSKASDNMMR DCDTLLMIGS SFPYAEWLPK EGQARGVEIN
IDGRMIGVRY PMEAYLVGDS RETLRALLPL LRRKDDRGWR KSVEKDVREW KELCAKRASQ
HFGGVINPQS VASALSDRLP ERAILTADSG SGTNWWARHL ELHDGMQASL SGTLATMGPG
VPYAIAARFA HPDRPVIAFV GDGAFQMNGM NEMITIKRYH KRLAGRAPFV FCVFNNRDLN
QVTWEQRAMA GDPKFPGSQD IPDVPYAAFA DLLGLRGIRC DEPRKVGRAW EEALSAKEPV
VLEFVVDPEI APIPPHIKTE QGKKAAKAMM HDPENIGIVA RGVRQKLTEY AAHLPGRGSS
//
