ID A0A0V1B9R0_TRISP Unreviewed; 1234 AA.
AC A0A0V1B9R0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN Name=Tktl2 {ECO:0000313|EMBL:KRY33331.1};
GN ORFNames=T01_15474 {ECO:0000313|EMBL:KRY33331.1};
OS Trichinella spiralis (Trichina worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6334 {ECO:0000313|EMBL:KRY33331.1, ECO:0000313|Proteomes:UP000054776};
RN [1] {ECO:0000313|EMBL:KRY33331.1, ECO:0000313|Proteomes:UP000054776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS3 {ECO:0000313|EMBL:KRY33331.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRY33331.1}.
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DR EMBL; JYDH01000084; KRY33331.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1B9R0; -.
DR eggNOG; KOG0523; Eukaryota.
DR Proteomes; UP000054776; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
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 Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001313; Pumilio_RNA-bd_rpt.
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; IPR005474; Transketolase_N.
DR PANTHER; PTHR43195:SF1; FI06132P-RELATED; 1.
DR PANTHER; PTHR43195; TRANSKETOLASE; 1.
DR Pfam; PF00806; PUF; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR Pfam; PF00456; Transketolase_N; 1.
DR SMART; SM00025; Pumilio; 4.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF48371; ARM repeat; 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 Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000054776};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 910..1089
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 78..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1234 AA; 137775 MW; C56868BE7B64BDEB CRC64;
MSHKFDSFLT LRIPSEPEKK FFDCKNSAVL HSKTGHKLCS PSFALSLFIA FSEGNEIFST
HARRRQNFTG RYFTHPAVEE SKKSPSSNQY SEQLSRTVQS DEANMSEEEK SILFKNLLSE
CHGHEISVLR EKDCFNNLLI IIGNNASIAM ELLWKIVKIR KKVILTLMTS YGGALEKLLA
VALNESEGPR KASVLLKLSE IALENVDSLS VQHGGSHLLR RLGSAISGVE KCAHNGATPI
FSAKNENEPK RFEANFLNQA EFISVYNNLA GRVLNWKSIR EFANREPFSL LVQDFIAFDS
SFNCTFVNGL LPSILEENKK TVHSMLTNKQ ASRVWDQYIR FSSIENVLKL YENCFRGSVA
RLISDQYANY PLQQMIRKVD DSVLAKELYE EVLQCFDEIW KARLYGVVHS LCIFVREKPQ
LETILVEKIK TVLNCRDPKI CEAHFLRCLL SMQCYVQDKK KIKYFGSVLT QTLATFSAKE
FFFEQMLNLP YEDFLQISSS SLGSYAVEAL VKAAETLDQR RAVVNKILPI TFKLANGRFG
SRVLECVWEN CDVEERLPIM DAMLKCSLKS QTVSKLNMKH DKCWSTARMP SALPDLHTIQ
ELKDIAHKLR IHSIRATNAS NSGHPTSCCS MAEIMSVLFF HTMKYDPKNP RDPYNDRFIL
SKGHAGPILY ACWVEAGLIP ESELLNLRKI DSDLEGHPTP RLSFVDVATG SLGQGLSCAA
GMAYVMKFMD KIDSRVYCVL GDGESAEGSV WEALHFAGMY ELDNLVAIFD INRLGQSQPA
SLGHRIDVYQ QRFEAFGWNV ECVDGHDVEA LCRSFSSAAG VKHKPTAIVA KTFKGFGIPK
VEDQENWHGK ALGKEAAAAL EAINSRIKNL DRHKLSINLP RIDPSKPLKA NDFSNVKLSE
PPNYKIGEKV ATRLAYGTAL VKLGKSCDRV IALDGDVKNS TFADKFKNAF PDRFIECFIS
EQNMQLAAAR EAERCLFVAP LLRFLQEHLI SFGWAPFLVP TSSAADRMQA CRLVSLFCSR
SIMQMYSLPC PGEDGPSQMG LEDIAMFRTL PGSTVFYPSD AVSCERAVEL AARVNGICFI
RTGRPNTPVI YSNEEQFSIG QAKIVRHSDK DRLMIVTAGV TLFEAFTAAD VLAKEKGLHV
CICDLFTVKP IDKRTLAEQA KRVGGKVLTV EDHYPEGGIG DAVASALAEY SDIQLKSLAV
NALPRSGPPD SLMDMFGISA KHIIEACVQL AGHA
//
