ID E1VI66_9GAMM Unreviewed; 342 AA.
AC E1VI66;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:CBL44508.1};
DE EC=1.2.4.1 {ECO:0000313|EMBL:CBL44508.1};
GN ORFNames=HDN1F_09250 {ECO:0000313|EMBL:CBL44508.1};
OS gamma proteobacterium HdN1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=83406 {ECO:0000313|EMBL:CBL44508.1, ECO:0000313|Proteomes:UP000002677};
RN [1] {ECO:0000313|EMBL:CBL44508.1, ECO:0000313|Proteomes:UP000002677}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HdN1 {ECO:0000313|Proteomes:UP000002677};
RA Widdel F., Rabus R., Grundmann O., Werner I., Schreiber F., Ehrenreich P.,
RA Behrends A., Wilkes H., Kube M., Reinhardt R., Zedelius J.;
RT "Alkane degradation by a new type of denitrifying bacterium with possible
RT involvement of the electron acceptor in substrate activation.";
RL Environ. Microbiol. 0:0-0(2010).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; FP929140; CBL44508.1; -; Genomic_DNA.
DR AlphaFoldDB; E1VI66; -.
DR STRING; 83406.HDN1F_09250; -.
DR KEGG; gpb:HDN1F_09250; -.
DR eggNOG; COG0022; Bacteria.
DR HOGENOM; CLU_012907_1_0_6; -.
DR OrthoDB; 9780894at2; -.
DR Proteomes; UP000002677; Chromosome.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
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 Oxidoreductase {ECO:0000313|EMBL:CBL44508.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002677};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 21..196
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 342 AA; 36872 MW; 9B528E0FB1FDB417 CRC64;
MGVNESIRGA TATIPSTSRI VTLVEAVNMA LHNAMEADPN VVVLGEDVGT NGGVFRATVG
LKERFGVKRV MDTPLAECMI GGISVGMATQ GLRPVAEIQF MGFALSALEH IISHAARIRN
RTRGRLSCPL VLRMPFGAGI HAPEHHSESL EALFAHIPGL RVVVPSSPAR AYGLLLSAIQ
DPDPVIFLEP TRIYRLIRQE VMDDGHGLPL DTCFTLQPGT DVTLVSWGAM VHETLQAAKS
LSKLGISAEV IDVATLAPLD MDTILHSVRK TGRCVIVHEA ARHCGVGAEI AARLAEKGLF
YLKAPIERVT GFDIPVPYSR NEGVYLPSSE DIVQACQRTM EY
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