ID A0A3N4SCZ5_9ACTN Unreviewed; 597 AA.
AC A0A3N4SCZ5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Pyruvate dehydrogenase (Quinone) {ECO:0000313|EMBL:RPE36520.1};
GN ORFNames=EDD38_4895 {ECO:0000313|EMBL:RPE36520.1};
OS Kitasatospora cineracea.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=88074 {ECO:0000313|EMBL:RPE36520.1, ECO:0000313|Proteomes:UP000266906};
RN [1] {ECO:0000313|EMBL:RPE36520.1, ECO:0000313|Proteomes:UP000266906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44781 {ECO:0000313|EMBL:RPE36520.1,
RC ECO:0000313|Proteomes:UP000266906};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (NOV-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:RPE36520.1}.
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DR EMBL; RKQG01000001; RPE36520.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4SCZ5; -.
DR Proteomes; UP000266906; 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:RPE36520.1};
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 200..328
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 388..543
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 597 AA; 65088 MW; 69C1225FC9367B5D CRC64;
MSRTVADQVL ARLREWGVEQ VFGYPGDGIN GLLAAWGRAD DRPAFVQARH EEMAAFEAVG
FAKFSGKVGV CAATSGPGAI HLLNGLYDAK LDHVPVVAIV GQTDRSAMGG SYQQEVDLLS
LYKDVASAYC QMVTVPQQLP NVLDRAFRTA AMYRTVTAVI IPADVQELPE QAPEHAFKMV
PSSLGMPHSH PVPDDGELLR AAEVLNAGGK VAMLVGQGAR GARQQVEQVA ELMGAGVAKA
LLGKDVLPDT LPYVTGSIGL LGTRPSYELM RDCDTLLTVG SSFPYTQFLP EFDQARAVQI
DADPFMVGLR YPYEVNLVGD AAATLDRLLP MLRRKKDRSW RKQVEKNTAR WWDVMEERAK
VPADPVNPEY LVHALDALLP EDAILTADSG SAANWYARHL RMRGTMRGSL SGTLATMGPG
VPYAIGAKFA HPDRPVVALV GDGAMQMNGL AELVTVARYR ERWSDPRLVV CVLNNHDLNQ
VTWEMRAMQG APSFLPSQQL PDVRYADFAE SVGLRGLRVE EPGKVRAAWE WALGADRPCV
LDVRTDPAVP PIPPHADWSQ IKDAAESVLR GDSDRVAVVK RGLRAKLAEL LPHRSRS
//
