ID A0A3Q8VB29_9ACTN Unreviewed; 580 AA.
AC A0A3Q8VB29;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Ubiquinone-dependent pyruvate dehydrogenase {ECO:0000313|EMBL:AZM59253.1};
GN ORFNames=DLM49_06500 {ECO:0000313|EMBL:AZM59253.1};
OS Streptomyces sp. WAC 01438.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2203204 {ECO:0000313|EMBL:AZM59253.1, ECO:0000313|Proteomes:UP000271045};
RN [1] {ECO:0000313|EMBL:AZM59253.1, ECO:0000313|Proteomes:UP000271045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAC 01438 {ECO:0000313|EMBL:AZM59253.1,
RC ECO:0000313|Proteomes:UP000271045};
RA Waglechner N., Wright G.D.;
RT "Evolution of GPA BGCs.";
RL Submitted (MAY-2018) 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; CP029601; AZM59253.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3Q8VB29; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000271045; Chromosome.
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:AZM59253.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000271045};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Ubiquinone {ECO:0000313|EMBL:AZM59253.1}.
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; 62743 MW; B38748FADCF3289C CRC64;
MAKQNIAEQF VDILTRAGVK RLYGVVGDSL NPVVDAVRRH AAIDWIHVRH EETAAFAAGA
EAQVTGRLAA CAGSCGPGNL HLINGLYDAH RSMAPVLALA SHIPSSEIGL GYFQETHPDQ
LFRECSHYSE LISSPRQMPR LLDTAIQHAV GRSGVSVVSL PGDLADEPAP DQAPETALVT
SRPTARPGDA EIDRLVDLID RAEKVTLFCG AGTKGAHAEV MEFAGKIKSP VGHALRGKEW
IQYDNPYDVG MSGLLGYGAA YEATHECDLL ILLGTDFPYN AFLPDDVKIV QVDVRPEILG
RRSKLDLAVW GDVKETLRCL TPRVRTKDDR KFLDRMLKKH ADALEGVVKA YTRKVEKHVP
IHPEYVASVL DELADDDAVF TVDTGMCNVW AARYITPNGR RRVIGSFSHG SMANALPMAI
GAQFTDRGRQ VVSMSGDGGF TMLMGDFLTL VQYDLPVKVV LFNNSSLSMV ELEMLVAGLP
SHGTAMKNPD FAAVARACGA YGVRVEKPKE LAGALKSAFR HKGPALVDVV TDPNALSIPP
KISKEMVTGF ALSASKVVLD GGVGRMLQMA RSNLRNVPRP
//
