ID A0A0N0SGK0_9ACTN Unreviewed; 580 AA.
AC A0A0N0SGK0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:KOU46068.1};
GN ORFNames=ADK54_14625 {ECO:0000313|EMBL:KOU46068.1};
OS Streptomyces sp. WM6378.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415557 {ECO:0000313|EMBL:KOU46068.1, ECO:0000313|Proteomes:UP000037774};
RN [1] {ECO:0000313|Proteomes:UP000037774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM6378 {ECO:0000313|Proteomes:UP000037774};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) 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:KOU46068.1}.
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DR EMBL; LGDD01000144; KOU46068.1; -; Genomic_DNA.
DR RefSeq; WP_053726054.1; NZ_LGDD01000144.1.
DR AlphaFoldDB; A0A0N0SGK0; -.
DR PATRIC; fig|1415557.3.peg.3267; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000037774; 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; 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.
PE 3: Inferred from homology;
KW Pyruvate {ECO:0000313|EMBL:KOU46068.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 192..320
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 383..529
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 580 AA; 62622 MW; D29CCC7B02BCCB0A CRC64;
MAKQNVAEQF VDILTRAGVK RLYGVVGDSL NPVVDAIRRN SAIDWIQVRH EEVAAFAAGA
EAQLTGKLAA CAGSCGPGNL HLINGLYDAH RSMAPVLALA SHIPSSEIGL GYFQETHPDQ
LFRECSHYSE LISNPQQMPR VLQTAIQHAI GRGGVSVLAL PGDIASEPAP DKAIDHALVT
SLPSVRPGDS EIDKLAALID EAKRVTLFCG SGTAGAHAEV MEFAERIKSP IGHALRGKEW
IQYDNKYDVG MSGLLGYGAA YEATHECDLL ILLGTDFPYN AFLPDDVKIV QVDVRPEHLG
RRSKLDLAVW GDVKETLRCL TPRVQVKTDR RFLDKMLKKH ADALEGVVKA YTRKVEKHVP
IHPEYVASVL DELAADDAVF TVDTGMCNVW AARYISPNGR RRIIGSFSHG SMANALPQAI
GAQFIDRGRQ VISMSGDGGF SMLMGDFLTL VQYELPVKIV LFNNSSLGMV ELEMLVAGLP
SYGTTNRNPD FAAIARAAGA YGVRVEKPKQ LAGALKDAFK HKGPALVDIV TDPNALSIPP
KISAEMVSGF ALSASKIVLD GGVGRMLQLA RSNLRNVPRP
//
