ID A0A1Y1I810_KLENI Unreviewed; 784 AA.
AC A0A1Y1I810;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=KFL_002080140 {ECO:0000313|EMBL:GAQ84837.1};
OS Klebsormidium nitens (Green alga) (Ulothrix nitens).
OC Eukaryota; Viridiplantae; Streptophyta; Klebsormidiophyceae;
OC Klebsormidiales; Klebsormidiaceae; Klebsormidium.
OX NCBI_TaxID=105231 {ECO:0000313|EMBL:GAQ84837.1, ECO:0000313|Proteomes:UP000054558};
RN [1] {ECO:0000313|EMBL:GAQ84837.1, ECO:0000313|Proteomes:UP000054558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2285 {ECO:0000313|EMBL:GAQ84837.1,
RC ECO:0000313|Proteomes:UP000054558};
RX PubMed=24865297; DOI=10.1038/ncomms4978;
RA Hori K., Maruyama F., Fujisawa T., Togashi T., Yamamoto N., Seo M.,
RA Sato S., Yamada T., Mori H., Tajima N., Moriyama T., Ikeuchi M.,
RA Watanabe M., Wada H., Kobayashi K., Saito M., Masuda T.,
RA Sasaki-Sekimoto Y., Mashiguchi K., Awai K., Shimojima M., Masuda S.,
RA Iwai M., Nobusawa T., Narise T., Kondo S., Saito H., Sato R., Murakawa M.,
RA Ihara Y., Oshima-Yamada Y., Ohtaka K., Satoh M., Sonobe K., Ishii M.,
RA Ohtani R., Kanamori-Sato M., Honoki R., Miyazaki D., Mochizuki H.,
RA Umetsu J., Higashi K., Shibata D., Kamiya Y., Sato N., Nakamura Y.,
RA Tabata S., Ida S., Kurokawa K., Ohta H.;
RT "Klebsormidium flaccidum genome reveals primary factors for plant
RT terrestrial adaptation.";
RL Nat. Commun. 5:3978-3978(2014).
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=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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
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DR EMBL; DF237157; GAQ84837.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1I810; -.
DR STRING; 105231.A0A1Y1I810; -.
DR OrthoDB; 5399939at2759; -.
DR Proteomes; UP000054558; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IBA:GO_Central.
DR GO; GO:0006098; P:pentose-phosphate shunt; IBA:GO_Central.
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; 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; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000054558};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 464..636
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 69..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 784 AA; 85051 MW; CCA193E164E06467 CRC64;
MASSQVIRGL TQSAALPLSS CSAQSAASAH VQLSPLPVQL SALPRDRTVK QHVSSKVLAS
EFSGLRLDSS AGCSTSGAQP PRSERRNRNG AARATATVGT DAQTLKKVDP KLSQRCITAI
RTLTVDSVEN AQAGHPGLPM GCAPIGYVLF DEVMKYNPKN PQWFNRDRFV LSAGHGVLLQ
YILLHLVGYD SVQVDDLKSL CKWGSRCPGH PENLLTGGIE LTTGPLGQGT ANAVGFAMAE
KHLAARFNRP GHEIVNHYTY CLAGDGCLME GISNEAGSMA GHLGLGKLIM FYDNNNNSID
GPTSITFDED VCKRYEALGW HVQRVGDPDS HLDDLRQAIV RAKSVTDKPS FIQVDTTIGY
GSPSKQGTAK AHHGTFGPEE VEKIRETLHA DYKEPFTVPQ DVLDHWRQNV TRGEQAEGEW
KQEWERYQRE YPEEARELDN LVNQRLPDDW ESVIPDFSGE TKGDATRGWS EKVINALAGR
VPGLIGGSAD LATSNKLYLK AWGDFEKDAP AERNIRYGVR EHAMAAISNG LALHRSGLIP
FAGTFFVFTD YMRGAVRISA LSDAGVIYVV THDSIGLGED GPTHQPVEHL ASLRAMPNMT
VVRPGDAIEV AGAYKVAIKN RSGPTMIVLS RQKLSSAVVS GTSADNVEKG GYVVSDNSEP
GKVPDLILLA TGAELELSEK AATKMREEAG FKVRLVSMVC WELFEAQPES YRNDVLPLEC
QARVSVEAGS KLGWREWVGP RGKIIAVDRF GASADYDTLF AKFGFSVDNI VSVSKQAIAE
AVPV
//
