ID A0A402DNQ0_9CELL Unreviewed; 354 AA.
AC A0A402DNQ0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE SubName: Full=Pyruvate dehydrogenase E1 component beta subunit {ECO:0000313|EMBL:GCE75757.1};
GN ORFNames=CBZ_08130 {ECO:0000313|EMBL:GCE75757.1};
OS Cellulomonas biazotea.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=1709 {ECO:0000313|EMBL:GCE75757.1, ECO:0000313|Proteomes:UP000289954};
RN [1] {ECO:0000313|EMBL:GCE75757.1, ECO:0000313|Proteomes:UP000289954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC12680 {ECO:0000313|EMBL:GCE75757.1,
RC ECO:0000313|Proteomes:UP000289954};
RA Yamamura H., Hayashi T., Hamada M., Serisawa Y., Matsuyama K., Nakagawa Y.,
RA Otoguro M., Yanagida F., Hayakawa M.;
RT "Draft genome sequence of Cellulomonas takizawaensis strain TKZ-21.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:GCE75757.1}.
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DR EMBL; BIMR01000043; GCE75757.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A402DNQ0; -.
DR OrthoDB; 3457658at2; -.
DR Proteomes; UP000289954; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR033248; Transketolase_C.
DR PANTHER; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Pyruvate {ECO:0000313|EMBL:GCE75757.1}.
FT DOMAIN 4..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 354 AA; 37628 MW; D817747247CB0B88 CRC64;
MTELTLARAL NAGLRRALED DPRVVLLGED IGRLGGVFRV TDGLQADFGP ERVRDTPLAE
AGIMGVAVGL AYRGFRPVVE IQFDGFVYPA FDQLVTQVAR LHYRTGGLVR MPITVRIPYG
GGIGAVEHHS ESPEAYFAHT PGLRVVTCGG PQDAHTMLRQ AVASDDPVVF LEPKRRYWVK
GEVDDSPADA LPLDRARVVV PGTDVTVAAY GPLVLTARDA ALAAADEGVS VEVVDLRSLA
PLDLDTLEAS VRRTGRLVVT HEAQRSGGLG AEVAASITER CFDVLHAPVA RVTGFDVPYP
PAKVEEHFLP GLDRLLDAVD RVMGRPHSLT GLTRAADPPA VAGVAAGFAS GRAS
//