ID A0A0M8WJG2_9NOCA Unreviewed; 581 AA.
AC A0A0M8WJG2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:KOV87209.1};
GN ORFNames=ADL03_07605 {ECO:0000313|EMBL:KOV87209.1};
OS Nocardia sp. NRRL S-836.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1519492 {ECO:0000313|EMBL:KOV87209.1, ECO:0000313|Proteomes:UP000037746};
RN [1] {ECO:0000313|Proteomes:UP000037746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL S-836 {ECO:0000313|Proteomes:UP000037746};
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:KOV87209.1}.
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DR EMBL; LGDY01000058; KOV87209.1; -; Genomic_DNA.
DR RefSeq; WP_053732623.1; NZ_LGDY01000058.1.
DR AlphaFoldDB; A0A0M8WJG2; -.
DR STRING; 1519492.ADL03_07605; -.
DR PATRIC; fig|1519492.3.peg.1660; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000037746; 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 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 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:KOV87209.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037746};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..124
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 196..322
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 385..531
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 581 AA; 61713 MW; E8892837DDACBED3 CRC64;
MTRTAADDLV DVLVNAGVRR IYGLVGDSLN AFSDAVRRRG GAAAGGIDWV HVHNEEAAAF
AASAEAQLTG RLAVCAGSCG PGNTHLVQGV MDAHRSGAPV LVLASHIASR QIGSGYFQET
DPKALFRQTA HYCEEVQRPD QLVRASRLAI QNALGKRGAA VLVLPGDVLA DDGTGEEVGD
LVRGRPVPAP DPEEVSELAG HIAGAHKIAI FAGIGCAEAR DEVLALAEHL RAPIGHTLRG
KDLLQHDNPF DVGMTGLLGY GACYRALHDA DLVLMLGTDF PYDDFLPGAR TVQVDVDPAR
LGRRTPLVQG IAADVGATLR ALLPLLDRRT DDGFLHDMLH RHERGIARSI ETYTGDHGQR
SPIHPEYLAR ILDETADEDA VFTVDTGMCC TWAARYLTPN GRRRILGSFV HGSMANALPM
AIGAQVAAPG RQVVSLSGDG GIAMLLGELL TVKTHRLPVK VVVFNNSSLG MVRLEMMVAG
DPPFETDHDE VDYAAIAAAA GFHTRRVTDP AELRAAVAEL LAHDGPALLD VVTTPDALEV
PSHVTLEEAR GFALSLGKTV LSGGIGKVYE LARQNLRNIP L
//
