TKT_NOSS1
ID TKT_NOSS1 Reviewed; 670 AA.
AC Q8YRU9;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Transketolase {ECO:0000250|UniProtKB:P23254, ECO:0000312|EMBL:BAB75043.1};
DE Short=TK {ECO:0000250|UniProtKB:P23254};
DE EC=2.2.1.1;
GN Name=tkt; OrderedLocusNames=alr3344;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1] {ECO:0000312|EMBL:BAB75043.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-20; 261-280 AND 491-510, AND MASS SPECTROMETRY.
RA Singh H., Rajaram H., Apte S.K.;
RL Submitted (DEC-2008) to UniProtKB.
CC -!- FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a
CC ketose donor to an aldose acceptor, via a covalent intermediate with
CC the cofactor thiamine pyrophosphate. {ECO:0000250}.
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:0000250|UniProtKB:P23254};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent
CC metal cations, such as Ca(2+), Mn(2+) and Co(2+). {ECO:0000250};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250|UniProtKB:P23254};
CC Note=Binds 1 thiamine pyrophosphate per subunit.
CC {ECO:0000250|UniProtKB:P23254};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=72000; Mass_error=1; Method=MALDI;
CC Evidence={ECO:0000269|Ref.2};
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000255}.
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DR EMBL; BA000019; BAB75043.1; -; Genomic_DNA.
DR PIR; AI2223; AI2223.
DR RefSeq; WP_010997495.1; NZ_RSCN01000038.1.
DR AlphaFoldDB; Q8YRU9; -.
DR SMR; Q8YRU9; -.
DR STRING; 103690.17132439; -.
DR EnsemblBacteria; BAB75043; BAB75043; BAB75043.
DR KEGG; ana:alr3344; -.
DR eggNOG; COG0021; Bacteria.
DR OMA; HHTEGIE; -.
DR OrthoDB; 188169at2; -.
DR Proteomes; UP000002483; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR CDD; cd02012; TPP_TK; 1.
DR Gene3D; 3.40.50.920; -; 1.
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; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR PANTHER; PTHR43522; PTHR43522; 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; SSF52518; 2.
DR SUPFAM; SSF52922; SSF52922; 1.
DR TIGRFAMs; TIGR00232; tktlase_bact; 1.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Magnesium; Metal-binding;
KW Reference proteome; Thiamine pyrophosphate; Transferase.
FT CHAIN 1..670
FT /note="Transketolase"
FT /id="PRO_0000366200"
FT ACT_SITE 416
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 31
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 71
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 120..122
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 389
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 443
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 467
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 475
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 528
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 31
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 268
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 670 AA; 72071 MW; A49796F6BA1A05B9 CRC64;
MAVATQSLEE LSINAIRFLA VDAIEKAKSG HPGLPMGAAP MAFVLWNRFM RYNPKNPKWF
NRDRFVLSAG HGSMLQYALL YLTGYDSVSI EDIKQFRQWE SKTPGHPENF MTAGVEVTTG
PLGQGIANGV GLAIAEAHLA AKFNKPDAKI VDHYTYVILG DGCNMEGVSG EAASFAGHLG
LGKLIALYDD NHISIDGSTD VAFTEDVSKR FESYGWHVIH VKDGNTDLEA IHKAIEEAKA
VTDKPTMIKV TTIIGYGSPN KSNTAGVHGA ALGGDEVALT RQNLGWSHDP FVVPEDVLNY
TRKAVERGAG YESDWNKTYA DYKAKYPQEA AEFERYLSGK LADGWDKVLP SYTPEDKGLP
TRKHSETCLN KLAAVLPELI GGSADLTHSN LTEIKGKGDF QKGQYQNPNI HFGVREHGMG
AICNGIALHG SGLIPYGATF LIFSDYMRAP IRLSALSQAG SIWVMTHDSI GQGEDGPTHQ
PIETLASLRA IPNLTVIRPA DGNETSGAYK VAIERAKNNA PTLLAFTRQN VPNLAGTSID
DVAKGGYIVV DTDGTPDLIL IGTGSELSLC VTAAEKLKAE GKKVRVVSLA AWDLFDAQDA
AYKESVLPKA VTKRLAVEAA SSFGWHKYIG SEGDAVTIDR FGASAPGGVC LEKFGFSVDN
VLAKAKQLLG
