ID A0A1I0L1K4_9ACTN Unreviewed; 588 AA.
AC A0A1I0L1K4;
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)/pyruvate oxidase {ECO:0000313|EMBL:SEU32943.1};
GN ORFNames=SAMN05421811_11199 {ECO:0000313|EMBL:SEU32943.1};
OS Nonomuraea wenchangensis.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=568860 {ECO:0000313|EMBL:SEU32943.1, ECO:0000313|Proteomes:UP000199361};
RN [1] {ECO:0000313|EMBL:SEU32943.1, ECO:0000313|Proteomes:UP000199361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5598 {ECO:0000313|EMBL:SEU32943.1,
RC ECO:0000313|Proteomes:UP000199361};
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; FOHX01000011; SEU32943.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0L1K4; -.
DR STRING; 568860.SAMN05421811_11199; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000199361; 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:SEU32943.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199361};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..116
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 201..331
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 391..538
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 588 AA; 63069 MW; 8E431AAEAD186A1A CRC64;
MTRIVAESLI ERLVAWGVDT VFGLPGDGIN GIMEGLRRHR DDVRFLLVHH EEAAAFMATA
HAKATGRIGV CLATSGPGGI HLLNGLYDAK LDHQPVLAIT GMQETSVLGT GYQQEVHLDR
LYEDVTEYNL LVDNPAQLPG VVDLAIRAAY ARRGVAHLTI PNDVQVAPAH EDPYPGVAPA
RPPATAPIYL SAPGVPRQED LEAAASVLNA ATRPAILAGA GALHARREVL AVADVLGAPV
IKTLPGKAVI PDDSPFAVGG IGLLGTRPGE ELVEDCDTLF MIGTNFPYTK HLPEPGQARV
VQLEADPVRA GVRMPTEVPM IGDAKQGLAA LLPLLERNGD RGHLAKYAKA MERWRADMAA
LRSSDRHPIA PQYLMACVDE VADDDAILTC DSGTIATWAA RHWTIRGERG FYLSGNLATM
APGLPYAVSM QHAFPGRQVI AFVGDGGFAM LMAEFLTAAQ HRLPIKVIVN NNNALGQILW
EQMVLGYPEH GVRFAEPAAD FSAWARSCGG YGRKVSDPRD LPEAVREALA HDGPALVDAD
VNPDEPPMPG KVTYEQAKKF AEAFLKGQPH KASIATTLFK DKISQMGR
//
