ID A0A286EKE2_9ACTN Unreviewed; 576 AA.
AC A0A286EKE2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Pyruvate dehydrogenase (Quinone) {ECO:0000313|EMBL:SOD71397.1};
GN ORFNames=SAMN05892883_0924 {ECO:0000313|EMBL:SOD71397.1};
OS Jatrophihabitans sp. GAS493.
OC Bacteria; Actinomycetota; Actinomycetes; Jatrophihabitantales;
OC Jatrophihabitantaceae; Jatrophihabitans.
OX NCBI_TaxID=1907575 {ECO:0000313|EMBL:SOD71397.1, ECO:0000313|Proteomes:UP000218903};
RN [1] {ECO:0000313|EMBL:SOD71397.1, ECO:0000313|Proteomes:UP000218903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAS493 {ECO:0000313|EMBL:SOD71397.1,
RC ECO:0000313|Proteomes:UP000218903};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) 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; LT907982; SOD71397.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A286EKE2; -.
DR InParanoid; A0A286EKE2; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000218903; Chromosome i.
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:SOD71397.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..115
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 191..318
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 394..540
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 576 AA; 61464 MW; F758DD3473EFC548 CRC64;
MTTVAEMIVE ALAEQGVRTV WGVVGDALNP ITDAIRRDER IEWLGVRHEE VGAFAAGAQA
QLTGTIGVCM GTVGPGSIHL LNGLYDAKKS HAPVLAICGQ VPLAELGSDY FQEVNNDLLF
TDVAVYSRTV TAAEQAPTML QAAIQAALQS PGVAVLTLPG DVGELELPKG TASPRIVAAH
PPTQPSAAAL AEATKLIDAA EKVTLLVGIG ARGARDELLA LARKLNAPMV LSLKAKPGLE
QDNPYQVGQS GLIGNPAASK AFDDCDLLLM VGTDFPYREW YPVGKTVVQV DVRAEQIGRR
TSVDLGLVGH AAPTLAALAA SVAPKDDELH LSKSREAYES WVKRQQVLTD PQRDKGLVGR
IRERFDNSED LIRPELLADL VGRQADEDAI FTTDTGMSTV WLSRFVTMSG RRELLGSFNL
GSMANAMPQA LGAQALDRRR QVIAFCGDGG LSMLLGDLIT AVSHNLPVKL FVFNNGRLGM
VKLEQEQGGL PEFGTVLDNP DFAQVARAIG LHANRVEDPL ALEQAVRDTL KQRGPALLDV
VTNPQEIALP GKVKQAQAWG FAIAKIRESV LSEGDS
//
