ID J4KRR2_9GAMM Unreviewed; 662 AA.
AC J4KRR2;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN Name=tkt {ECO:0000313|EMBL:EJP71399.1};
GN ORFNames=NT01SARS_1206 {ECO:0000313|EMBL:EJP71399.1};
OS SAR86 cluster bacterium SAR86A.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; SAR86 cluster.
OX NCBI_TaxID=1123866 {ECO:0000313|EMBL:EJP71399.1, ECO:0000313|Proteomes:UP000010305};
RN [1] {ECO:0000313|EMBL:EJP71399.1, ECO:0000313|Proteomes:UP000010305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22170421; DOI=10.1038/ismej.2011.189;
RA Dupont C.L., Rusch D.B., Yooseph S., Lombardo M.J., Richter R.A., Valas R.,
RA Novotny M., Yee-Greenbaum J., Selengut J.D., Haft D.H., Halpern A.L.,
RA Lasken R.S., Nealson K., Friedman R., Venter J.C.;
RT "Genomic insights to SAR86, an abundant and uncultivated marine bacterial
RT lineage.";
RL ISME J. 6:1186-1199(2012).
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=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
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}.
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DR EMBL; JH611157; EJP71399.1; -; Genomic_DNA.
DR AlphaFoldDB; J4KRR2; -.
DR STRING; 1123866.NT01SARS_1206; -.
DR HOGENOM; CLU_009227_0_0_6; -.
DR Proteomes; UP000010305; Unassembled WGS sequence.
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:UP000010305};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EJP71399.1}.
FT DOMAIN 353..524
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 662 AA; 73689 MW; 1B5AB06333EEC490 CRC64;
MQQSDHINVL RFLSADAVQK ANSGHPGMPM GMAEIATALW SKHLRHNPKN PTWFNRDRFV
LSNGHGSMLL YSLLHLTGYD LSINDIKDFR KLKSKTPGHP EYDIDIGIET TTGPLGQGIA
NAVGMAVAEK ILAAEFNKDD IKPIDHFTYV FLGDGCLMEG ISHEACSFAG THNLGKLICF
YDQNGISIDG EIEHWFTDDS VKRFESYGWQ TICVDGHDIE DIDGAIHKAK EEVNKPTMIF
CKTTIGYGSP NKSGTADVHG APLGDEELKE TREVLGWNYK PFEVPQEVYD FWNFKEEGAS
FNDSWNKLLK DYEKKYPNDS LELHRRIDGH LPNNFQESYE SFLNECNSNN LSMATRKASK
ACLDFFVKEM PELIGGSADL TPSNNTFSSS SSTFSNENAS GNHINYGVRE FGMSAIMNGM
VLHGAIKPYG ATFLVFTDYA RNAVRLSALM KLPNIFVYTH DSVALGEDGP THQPIEHMVT
LRSTPNLNNW RPADLVETAV SWKSAVSSQK TPTCLIYSRQ GTSAIKRSPD QISMIDMGGY
LLEESDDFDL TIVASGSEVQ LALDAAKELK NDSINANVVS MPCLDIFLDQ DKEYQNKIIN
PEKPVLVVEC AHPNSWYRIL NRNDKVIGIE TFGESAPGSE LLNHFGFNTD NVIKTAKSLI
ND
//
