ID G4Q8K4_ACIIR Unreviewed; 663 AA.
AC G4Q8K4;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN Name=tktA {ECO:0000313|EMBL:AEQ21633.1};
GN OrderedLocusNames=Acin_0390 {ECO:0000313|EMBL:AEQ21633.1};
OS Acidaminococcus intestini (strain RyC-MR95).
OC Bacteria; Bacillota; Negativicutes; Acidaminococcales; Acidaminococcaceae;
OC Acidaminococcus.
OX NCBI_TaxID=568816 {ECO:0000313|EMBL:AEQ21633.1, ECO:0000313|Proteomes:UP000007093};
RN [1] {ECO:0000313|EMBL:AEQ21633.1, ECO:0000313|Proteomes:UP000007093}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RyC-MR95 {ECO:0000313|EMBL:AEQ21633.1,
RC ECO:0000313|Proteomes:UP000007093};
RX PubMed=22123762; DOI=10.1128/JB.06301-11;
RA D'Auria G., Galan J.C., Rodriguez-Alcayna M., Moya A., Baquero F.,
RA Latorre A.;
RT "Complete genome sequence of Acidaminococcus intestini RYC-MR95, a Gram-
RT negative bacterium from the phylum Firmicutes.";
RL J. Bacteriol. 193:7008-7009(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737,
CC ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001027};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003058; AEQ21633.1; -; Genomic_DNA.
DR RefSeq; WP_009016006.1; NC_016077.1.
DR AlphaFoldDB; G4Q8K4; -.
DR STRING; 568816.Acin_0390; -.
DR KEGG; ain:Acin_0390; -.
DR PATRIC; fig|568816.4.peg.381; -.
DR eggNOG; COG0021; Bacteria.
DR HOGENOM; CLU_009227_0_0_9; -.
DR InParanoid; G4Q8K4; -.
DR Proteomes; UP000007093; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR CDD; cd02012; TPP_TK; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR005478; Transketolase_bac-like.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR049557; Transketolase_CS.
DR InterPro; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR NCBIfam; TIGR00232; tktlase_bact; 1.
DR PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR PANTHER; PTHR43522:SF2; TRANSKETOLASE 1-RELATED; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR Pfam; PF00456; Transketolase_N; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000007093};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 352..523
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 663 AA; 72089 MW; 28BE4779413A9A0C CRC64;
MKKIDQESIN TLRFLSIDEV QAANSGHPGL PLGTAPLMYT IWDRFMKVNP KDPSWFDRDR
FVLSPGHGSA LQYAMLHLAG YKVSLDDLKQ FRQWGSLTPG HPEYGVTPGV DVSTGPLGHG
FAMAVGLAMA EKMLAARYNK KGFPVVDHYT YGITSDGDQM EGVASEAASL AGTLGLGKLI
FLYDDNKITI EGHTDIAFKE DVGARFVAYG WQVLRVSTSE DVEELAKAIK EAKREKNRPS
LIIVPTHIGF GSPRQDMASA HGEPLGAENV AATKKAAGWD PEKSFYVPDE VRAHFEEKIP
AAERKEAEWE ALLDEYAKKY PDLAAELVDR MNGKVDLDLK KLMAIFDGTE SAATRAASGT
VLQSLADALP SLVGGSADLG PSNKTEMKGK GFFSARTPEG RNIHFGIREH AMGCIVNGLS
LHGGLLPFGA TFLVFADFMR PAIRMAALMG IGSHFVFTHD SIFVGEDGPT HQPVEQAMSL
RLIPNVSVIR PADALETAAA WKTACETKDR PTCLLLTRQG MPVLHDYAKV IAKGAPKGAY
ILSPCPKEED LKAVIIATGS EVHLALEAQK KLTKRHIGVQ VVSMPSWDLF DSQSAAYRRR
VLPKDVPAIA VEAGVRTGWA RYTGSEDHVI GIDTFGASGP GKTVYKEYGF TVDHIVDMVR
KVK
//
