ID R7WTM7_9NOCA Unreviewed; 590 AA.
AC R7WTM7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:EOM78607.1};
GN ORFNames=Rrhod_0145 {ECO:0000313|EMBL:EOM78607.1};
OS Rhodococcus rhodnii LMG 5362.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1273125 {ECO:0000313|EMBL:EOM78607.1, ECO:0000313|Proteomes:UP000013525};
RN [1] {ECO:0000313|EMBL:EOM78607.1, ECO:0000313|Proteomes:UP000013525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 5362 {ECO:0000313|EMBL:EOM78607.1,
RC ECO:0000313|Proteomes:UP000013525};
RX PubMed=23788540;
RA Pachebat J.A., van Keulen G., Whitten M.M., Girdwood S., Del Sol R.,
RA Dyson P.J., Facey P.D.;
RT "Draft Genome Sequence of Rhodococcus rhodnii Strain LMG5362, a Symbiont of
RT Rhodnius prolixus (Hemiptera, Reduviidae, Triatominae), the Principle
RT Vector of Trypanosoma cruzi.";
RL Genome Announc. 1:e00329-13(2013).
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:EOM78607.1}.
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DR EMBL; APMY01000003; EOM78607.1; -; Genomic_DNA.
DR AlphaFoldDB; R7WTM7; -.
DR PATRIC; fig|1273125.3.peg.144; -.
DR eggNOG; COG0028; Bacteria.
DR Proteomes; UP000013525; 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; IPR000399; TPP-bd_CS.
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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Pyruvate {ECO:0000313|EMBL:EOM78607.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000013525};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 194..323
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 386..532
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 590 AA; 62418 MW; 29EC894D0D900125 CRC64;
MGTVADQLVE QLVAAGVRRI YGIVGDSLNP VVDAVRRSGG RARGGIDWVH VRHEEAAAFA
ASAEAQLTGE LAVCAGSCGP GNLHLINGLY DANCSDAPVL AIASHIPSAQ IGMEYFQETH
PDRLFVECSQ YCELVSTPQQ APRVFASAIT HAVARSGVSV VTLPGDVAED DAVRTAPAPV
RLGRPTLVPD PADVQALAAL VDDARNVAIF AGDGVRDARD AVLAFADAVG APIGHSLRGK
NWIQYDNPFD VGMTGLLGYG AAHDGIHDAD LLVLVGTDFP YDQFLPQSDV KVAQIDTAAE
RIGRRTSVDV AVHGDARATF EALLPLVRRK SDRSFLDDTL DRHRKLMSQV VGGYAESANQ
RTPIHPEYAA SVLDDLAADD AVFTADTGMC NVWTARYVTP NGRRMLVESA LHGSMANALP
HAIGASFADP QRQVISVSGD GGLSMLLGEL LTVVMYRIPV KIVLFDNSSL GMVKLEMLVD
GLPDFGVDVP GVDYAAIAQA MGIFARRIED PGDVESGLRA VLEHDGPALA DVVTDPRALS
LPPTITGSQV GGFARAMSKV VMNGGVGEAV QMAKSNLRNM PRPSQFDPRT
//
