ID R1FB68_EMIHU Unreviewed; 646 AA.
AC R1FB68;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:EOD30484.1};
GN Name=TK {ECO:0000313|EMBL:EOD30484.1};
GN ORFNames=EMIHUDRAFT_423965 {ECO:0000313|EMBL:EOD30484.1};
OS Emiliania huxleyi (Coccolithophore) (Pontosphaera huxleyi).
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Isochrysidales;
OC Noelaerhabdaceae; Emiliania.
OX NCBI_TaxID=2903 {ECO:0000313|EMBL:EOD30484.1};
RN [1] {ECO:0000313|EMBL:EOD30484.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP1516 {ECO:0000313|EMBL:EOD30484.1};
RG DOE Joint Genome Institute;
RA Read B., Kegel J., Klute M., Kuo A., Lefebvre S.C., Maumus F., Mayer C.,
RA Miller J., Allen A., Bidle K., Borodovsky M., Bowler C., Brownlee C.,
RA Claverie J.-M., Cock M., De Vargas C., Elias M., Frickenhaus S.,
RA Gladyshev V.N., Gonzalez K., Guda C., Hadaegh A., Herman E.,
RA Iglesias-Rodriguez D., Jones B., Lawson T., Leese F., Lin Y.-C.,
RA Lindquist E., Lobanov A., Lucas S., Malik S.-H.B., Marsh M.E., Mock T.,
RA Monier A., Moreau H., Mueller-Roeber B., Napier J., Ogata H., Parker M.,
RA Probert I., Quesneville H., Raines C., Rensing S., Riano-Pachon D.M.,
RA Richier S., Rokitta S., Salamov A., Sarno A.F., Schmutz J., Schroeder D.,
RA Shiraiwa Y., Soanes D.M., Valentin K., Van Der Giezen M., Van Der Peer Y.,
RA Vardi A., Verret F., Von Dassow P., Wheeler G., Williams B., Wilson W.,
RA Wolfe G., Wurch L.L., Young J., Dacks J.B., Delwiche C.F., Dyhrman S.,
RA Glockner G., John U., Richards T., Worden A.Z., Zhang X., Grigoriev I.V.;
RT "Genome variability drives Emilianias global distribution.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000013827}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP1516 {ECO:0000313|Proteomes:UP000013827};
RX PubMed=23760476; DOI=10.1038/nature12221;
RA Read B.A., Kegel J., Klute M.J., Kuo A., Lefebvre S.C., Maumus F.,
RA Mayer C., Miller J., Monier A., Salamov A., Young J., Aguilar M.,
RA Claverie J.M., Frickenhaus S., Gonzalez K., Herman E.K., Lin Y.C.,
RA Napier J., Ogata H., Sarno A.F., Shmutz J., Schroeder D., de Vargas C.,
RA Verret F., von Dassow P., Valentin K., Van de Peer Y., Wheeler G.,
RA Dacks J.B., Delwiche C.F., Dyhrman S.T., Glockner G., John U., Richards T.,
RA Worden A.Z., Zhang X., Grigoriev I.V., Allen A.E., Bidle K., Borodovsky M.,
RA Bowler C., Brownlee C., Cock J.M., Elias M., Gladyshev V.N., Groth M.,
RA Guda C., Hadaegh A., Iglesias-Rodriguez M.D., Jenkins J., Jones B.M.,
RA Lawson T., Leese F., Lindquist E., Lobanov A., Lomsadze A., Malik S.B.,
RA Marsh M.E., Mackinder L., Mock T., Mueller-Roeber B., Pagarete A.,
RA Parker M., Probert I., Quesneville H., Raines C., Rensing S.A.,
RA Riano-Pachon D.M., Richier S., Rokitta S., Shiraiwa Y., Soanes D.M.,
RA van der Giezen M., Wahlund T.M., Williams B., Wilson W., Wolfe G.,
RA Wurch L.L.;
RT "Pan genome of the phytoplankton Emiliania underpins its global
RT distribution.";
RL Nature 499:209-213(2013).
RN [3] {ECO:0000313|EnsemblProtists:EOD30484}
RP IDENTIFICATION.
RG EnsemblProtists;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
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DR EMBL; KB864700; EOD30484.1; -; Genomic_DNA.
DR RefSeq; XP_005782913.1; XM_005782856.1.
DR STRING; 2903.R1FB68; -.
DR PaxDb; 2903-EOD30484; -.
DR EnsemblProtists; EOD30484; EOD30484; EMIHUDRAFT_423965.
DR GeneID; 17275757; -.
DR KEGG; ehx:EMIHUDRAFT_423965; -.
DR eggNOG; KOG0523; Eukaryota.
DR HOGENOM; CLU_009227_0_0_1; -.
DR OMA; ADYMRGS; -.
DR Proteomes; UP000013827; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR PANTHER; PTHR43522:SF2; TRANSKETOLASE 1-RELATED; 1.
DR Pfam; PF02779; Transket_pyr; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000013827}.
FT DOMAIN 335..505
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 196..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 646 AA; 69223 MW; 8BF70248224A4CA1 CRC64;
MVQAANSGHP GAPMGCAPMA HVLWSGVMSY DPADPEWINR DRFVLSNGHA CALLYSMLHL
TGYGVSIDDL KQFRQLDSIT PGHPENGVTP GVEVSTGPLG QGISNGVGLA MAQAHLGATF
NREGFSLIDN FTYVICGDGC MQEGISSEAV VLVGHLQLGR LIVLYDDNKI QIDGATSLAF
SEDVGKRYEA YGWQASAPRS AAPRHTTTHT HTPPAASGSS HLRREGDTSR VQYEWLRRIT
GQPLPGRPQQ QPPFGRSGGA EQAVFVAADD DQSALLGEYA AAHPALAAEF ERRRAGELPA
GWREARRFLP AAARSKPPPP HPAAALASLE WDKPLATRQS SQLVLNKLCE VVPELVGGSA
DLTPSNLTKF KGAADFQAPS PHPLAPRHAA SPEGRYIRFG VREHAMAALC NGMHAYGMLR
PFCATFLNFF GYAAGAVRVS ALSHFGEDGP THQPVEALVN LRATPNLLTL RPADANEVVG
AYMVAMERPK TPAVIALSRQ GCANLAGSRA EAVARGAYDT PPQLVLVGTG SEVQTLEQAV
PLLEGVRVQL VSMPCCELFD SQPREYKHEV LPPGVPVLAM EALAAEGWCK YAHSVIGMRS
FGCSAPAKEV QKRFGFTADN AALRARELLQ HYANKLAPDL LDRPDN
//
