ID A0A101TCT4_9ACTN Unreviewed; 580 AA.
AC A0A101TCT4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:KUN89785.1};
GN ORFNames=AQJ66_01535 {ECO:0000313|EMBL:KUN89785.1};
OS Streptomyces bungoensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=285568 {ECO:0000313|EMBL:KUN89785.1, ECO:0000313|Proteomes:UP000053024};
RN [1] {ECO:0000313|EMBL:KUN89785.1, ECO:0000313|Proteomes:UP000053024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 41781 {ECO:0000313|EMBL:KUN89785.1,
RC ECO:0000313|Proteomes:UP000053024};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces bungoensis DSM 41781, type strain
RT for the species Streptomyces bungoensis.";
RL Submitted (OCT-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:KUN89785.1}.
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DR EMBL; LMWX01000003; KUN89785.1; -; Genomic_DNA.
DR RefSeq; WP_061915185.1; NZ_KQ948851.1.
DR AlphaFoldDB; A0A101TCT4; -.
DR STRING; 285568.AQJ66_01535; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000053024; 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:KUN89785.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053024};
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 193..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; 62800 MW; D42EC26E257E2AD0 CRC64;
MAKQNVAEQF VDILVRAGVR RLYGVVGDSL NPVVDAVRRN SAIDWIHVRH EESAAFAAGA
EAQITGKLAA CAGSCGPGNL HLINGLYDAH RSMAPVLALA SHIPSSEIGL GYFQETHPDR
LFLECSHYSE LISSPKQMPR LLQTAVQHAV GQRGVSVVSL PGDIAGEPAP EKAPQSALVT
SRPTVRPGDA ELDRLVEMID AARRVTLFCG AGTAGAHAEV MEFAGRIKSP VGHALRGKEW
IQYDNPFDVG MSGLLGYGAA YEATHECDLL ILLGTDFPYN AFLPDDVRIA QIDVRPEVLG
RRSRLDLAVW GDVRETLRCL VPRVKEKTDR RFLDRMLKKH ADALEGVVKA YTRKVEKHVP
IHPEYVAAVL DEVAADDAVF TIDTGMCNVW GARYISPNGR RRIIGSFSHG SMANALPMAI
GAQFTDRRRQ VVAMSGDGGF AMLMGEFLTL VQHDLPVKVV LFNNSSLGMV ELEMLVAGLP
SYGTRNSNPD FAAVARACGA YGIRVERPKQ LAGALKDAFR HKGPALVDVV TDPNALSIPP
KISAEMVTGF ALSASKIVLE GGVGRMLQMA RSNLRNVRRP
//
