ID A0A022LIH9_9ACTN Unreviewed; 703 AA.
AC A0A022LIH9;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=H483_0106625 {ECO:0000313|EMBL:EYT63595.1};
OS Dietzia sp. UCD-THP.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Dietziaceae;
OC Dietzia.
OX NCBI_TaxID=1292020 {ECO:0000313|EMBL:EYT63595.1, ECO:0000313|Proteomes:UP000019757};
RN [1] {ECO:0000313|EMBL:EYT63595.1, ECO:0000313|Proteomes:UP000019757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-THP {ECO:0000313|EMBL:EYT63595.1,
RC ECO:0000313|Proteomes:UP000019757};
RX PubMed=23661480;
RA Diep A.L., Lang J.M., Darling A.E., Eisen J.A., Coil D.A.;
RT "Draft Genome Sequence of Dietzia sp. Strain UCD-THP (Phylum
RT Actinobacteria).";
RL Genome Announc. 1:E00197-E00113(2013).
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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
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:EYT63595.1}.
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DR EMBL; AOSR01000023; EYT63595.1; -; Genomic_DNA.
DR RefSeq; WP_031264866.1; NZ_KB714650.1.
DR AlphaFoldDB; A0A022LIH9; -.
DR eggNOG; COG0021; Bacteria.
DR HOGENOM; CLU_009227_0_0_11; -.
DR Proteomes; UP000019757; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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; IPR020826; Transketolase_BS.
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.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 375..555
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 703 AA; 75100 MW; 2DA0EF44481A1DB9 CRC64;
MTSASEITEL TTARHPSDWT ELDTRAVDTA RVLAAEAVQN CGSGHPGTAM SLAPLAYTLY
QRVMRHDPSD PKWVGRDRFV LSCGHTSLTQ YIQLYLAGFG LELEDLKALR TWGSKTPGHP
EWNHTDGVEI TTGPLGQGLA SAVGMAMAAR YERGLFDPDA PAGKSPFDHF VYVIASDGDV
QEGVTAEACS LAGTQQLGNL IAIYDDNKIS IEDDTQIAFT EDVAARYEAY GWHVQTVHGG
EDIEAIEDAI ADARAVTDKP SIIVLRTVIA YPAPTKMNTG ASHGSALGQA EVDAVKEALG
MGGTEPFTVD DEVIAHTRAA RDRGARVHAQ WSDMFHEWAE ANPGAKDLFD RLYSGQLPEG
WDADLPRWEA DPKGVATRKA SAKAIQALAG TLPELWGGSA DLAGSNNTQI EGADSFGPPS
ISTGTWTASP YGRNLHFGVR EHAMGAILNG IALHGPTRPY GGTFLIFSEY MRPAVRLAAL
QGSNAYYVWT HDSIGLGEDG PTHQPVEQLA ALRAIPGLAV LRPADANETA AAWRAMLVAL
DGPKGLCLTR QDIPVLEGTA ESAREGVERG GYVIAEASTG SPEVILMGTG SEVHLAVEAR
EVLEAEGVAT RVVSMPCIEF FDQQDPEYRE SVLPRSVRAR VSVEAGISMP WYRFLGDAGR
AVSLEHFGAS APYQTLYTEF GITADAVVTA ARESLAAVTG ESS
//
