ID A6YB00_KARVE Unreviewed; 576 AA.
AC A6YB00;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:ABQ23347.1};
DE Flags: Fragment;
OS Karlodinium veneficum (Dinoflagellate) (Karlodinium micrum).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Gymnodiniales; Kareniaceae;
OC Karlodinium.
OX NCBI_TaxID=407301 {ECO:0000313|EMBL:ABQ23347.1};
RN [1] {ECO:0000313|EMBL:ABQ23347.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17562012; DOI=10.1186/1471-2148-7-89;
RA Rogers M.B., Watkins R.F., Harper J.T., Durnford D.G., Gray M.W.,
RA Keeling P.J.;
RT "A complex and punctate distribution of three eukaryotic genes derived by
RT lateral gene transfer.";
RL BMC Evol. Biol. 7:89-89(2007).
RN [2] {ECO:0000313|EMBL:ABQ23347.1}
RP NUCLEOTIDE SEQUENCE.
RA Rogers M.B., Watkins R.F., Harper J.T., Durnford D.G., Gray M.W.,
RA Keeling P.J.;
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
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; EF216683; ABQ23347.1; -; mRNA.
DR AlphaFoldDB; A6YB00; -.
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 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; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR PANTHER; PTHR43522:SF10; TRANSKETOLASE; 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 2: Evidence at transcript level;
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 264..440
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABQ23347.1"
SQ SEQUENCE 576 AA; 61833 MW; BE9F1FD156324F06 CRC64;
TRMTPGHPEF PSSEHNTPGI EATTGPLGAG IGNAVGMAAA AKLAAAKYNT EQHEIFDHHV
IALCGDGCLQ EGVSFEAASF AGHDGLDNLI LIYDQNDVTL DKMADFTQGV DHAKYFESLG
WNVISIDGHD LKAVDDSIVK AKSTKNGKPT LIIAKTVIGQ GVEEIEGTNA AHGEAGVAYQ
ESARKNLGLP AGDLFYVDPE TRKFFEGRKA DLKANYNAWT EKFNAWKEAN PDLAKDLEVA
SSKSTPSIEE LSAGIPEYDS SKNVATRQSG SDVLQFIAKM VPQYVSGSAD LHGSNKNYIN
DGKNFGNPKI EGKSFDGRNF YFGIREHAMG TMLNGMAYYG LNIPSGSTFL VFADYMRAAI
RVAALSELPT SYILTHDSVG VGEDGPTHQP VEATSGLRII PNLDVMRPAD PEEVAGAFMA
SVDRKDGPTA LILSRQNVRT LNEISVADRR MGTLKGGYVA LKETGDLKMI LLASGSELQW
AMDAAKDLGD GVRVVSMPCF ERFDRQDAAY KAEVLPSSCT KRVAIEAGVS GLWYKYVGLD
GKVIGTDKFG FSAPGDTVMK AFGLNAENLV EVAKSM
//
