ID R7WPB7_9NOCA Unreviewed; 702 AA.
AC R7WPB7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=Rrhod_2877 {ECO:0000313|EMBL:EOM75804.1};
OS Rhodococcus rhodnii LMG 5362.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1273125 {ECO:0000313|EMBL:EOM75804.1, ECO:0000313|Proteomes:UP000013525};
RN [1] {ECO:0000313|EMBL:EOM75804.1, ECO:0000313|Proteomes:UP000013525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 5362 {ECO:0000313|EMBL:EOM75804.1,
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 -!- 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:EOM75804.1}.
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DR EMBL; APMY01000082; EOM75804.1; -; Genomic_DNA.
DR RefSeq; WP_010838921.1; NZ_APMY01000082.1.
DR AlphaFoldDB; R7WPB7; -.
DR PATRIC; fig|1273125.3.peg.2747; -.
DR eggNOG; COG0021; Bacteria.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000013525; 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 Reference proteome {ECO:0000313|Proteomes:UP000013525};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 375..560
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 702 AA; 75601 MW; 31404B2261A70514 CRC64;
MSTTDEIRDL TTAVHPEDWT ELDTKAVDTV RVLAADAVQK VGNGHPGTAM SLAPLAYTLF
QRVMRHDPAD ADWIGRDRFV LSCGHSSLTL YIQLYLAGYG LELSDLEQLR TWDSKTPGHP
EHGHTRGVEI TTGPLGQGLA SAVGMAMSAR RQRGLFDPEA PAGESPFDHH VYVVASDGDL
QEGVTSEASS LAGTQQLGNL TVIYDDNKIS IEDDTTIAFT EDTAARYEAY GWHVQVVEGG
EDVVAIENAL KAAREVTDKP SLILLRTIIG FPAPDKMNTG AAHGAALGAD EVAKVKEVLG
FDPEQNFQVD EKVIAHTREA LVRGATAHRE WQGSFDAWAE RNPENAALLE RLSTYGLPDG
WTDALPAFDT DPSGMATRKA SASFLQAVGD VLPELWGGSA DLAESNNTTI KGSDSFGPES
ISTTMWSARP YGRTLHFGVR EHAMGSILNG IALAGPTRPY GGTFLVFSDY MRPAVRLAAL
MKLGVTYVWT HDSIGLGEDG PTHQPIEHLA ALRAIPGLSV VRPADANETV HAWRTTLERG
SIDQTRGPVG LALTRQNVPV LEGTSYDGVK RGGYVLTDAS NGVPEVILVA TGSEVQLAVA
ARETLEADGV PTRVVSMPCL EWFEEQDEAY RDGVLPPTVK ARVVVEAGIA MPWYRYVGSE
GEIVSIEHFG ASADFETLFR EFGFTPETVT AAAQRSLARV KG
//
