ID A0A0N5BKU3_STREA Unreviewed; 607 AA.
AC A0A0N5BKU3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
OS Strongyloides papillosus (Intestinal threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0000654800.1};
RN [1] {ECO:0000313|WBParaSite:SPAL_0000654800.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A0N5BKU3; -.
DR STRING; 174720.A0A0N5BKU3; -.
DR WBParaSite; SPAL_0000654800.1; SPAL_0000654800.1; SPAL_0000654800.
DR Proteomes; UP000046392; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
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; 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; 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 Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 302..466
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 607 AA; 64644 MW; 9CD0D8570D4972A1 CRC64;
MPANIGALKD VANRLRIASI EMTAVAKSGH PSSSTSAAEI VATLFFNEMK YEVASPKAPY
SDRFVLSKGH ACPILYAAWE EAGLLSHEQI LSLRKIDSDI EGHPTPRLNF IDVATGSLGQ
GLSIAVGMAW VGKYKDKASY RVYALLGDGE TAEGSIWEAA AFAITIVDVN RLGQSQETQL
GHEVETYAAR FKAFGHNAII VDGHDIEALL NAFATARNTK DKPTAIIAKT FKGAGIEGVE
NLENWHGKPV PMEKIEAIKS KLSSTQKGSI PIPSPIKDTP EFDLNLGNIK IAPPSYKLGD
KVATRAAYGT ALAKLGDASP HVIGLDGDTK NSTFSDKLLA KYPERFIECF IAEQNLVGVG
IGVGCRGRAI PFCSTFAAFF TRAADQLRMG AISFANLKCA GSHAGISIGE DGPSQMALED
LSLFRSVANS VVLYPTDAVS AERAAELAAN IHGIVFIRTG RPALPVIYNN DEPFAIGKAK
VVRKSDKDSI LLVGAGVTLY ECIKAADELA SSGINACIID IFSVKPIDQQ TLINEAKRCG
GKVITVEDHY QSGGLGEAVS SALADTSNVR VRSIFVRDIP RSGSPEGLLD LFGISAPHIV
KAVKNFN
//
