ID A0A016SED9_9BILA Unreviewed; 631 AA.
AC A0A016SED9;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN Name=Acey_s0243.g3484 {ECO:0000313|EMBL:EYB88659.1};
GN Synonyms=Acey-tkt-1 {ECO:0000313|EMBL:EYB88659.1};
GN ORFNames=Y032_0243g3484 {ECO:0000313|EMBL:EYB88659.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB88659.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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:EYB88659.1}.
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DR EMBL; JARK01001579; EYB88659.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016SED9; -.
DR STRING; 53326.A0A016SED9; -.
DR Proteomes; UP000024635; 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: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 Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 327..491
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 631 AA; 67913 MW; 307657BCDCFCD754 CRC64;
MLRLSNVLRS WVAKMPISAE LRNDLEDCAN RMRISAIEMT CASKSGHPTS STSAAEVVST
LFFHEMKYDI ANPKCPSADR FVLSKGHACP ILYAAWEEAG LLSKDQVMSL RKINSDIEGH
PTPRLNFIDV ATGSLGQGLS CAAGMAYVGK YIDKASYRVY CLMGDGETAE GAVWEAAAFS
SKYKLDNLVA IVDVNRLGQS QETALGHHVE IYQARFAAFG FEAIIVNGHD VEEIITAFER
ARNTKDKPTA IIAKTLKGMG IDGIADQENW HGKPVPADKV NAIKARLHGS QKGKLVAKKP
AGDAPKVDLQ IGSIKMAPPN YKKGDKVATR AAYGTALAKL GDANPRVIGL DGDTKNSTFS
EKLLQKHPNQ FIECYIAEQN LVGVAVGAQC RDRTIPFTST FAAFFTRACD QIRMAAVSFA
NLKCAGSHVG VSIGEDGPSQ MALEDLAMFR ALPGSTVFYP TDGVSAERAT ELAANIKGIV
FIRTGRPALP VLYANDEPFA VGKAKVLKQS PGDKIVLIGA GVTTYECMKA AEQLEKEGVN
CCIIDPFTIK PLDQATIVEH ANRVGGRILT VEDHYPAGGI GETVSAAVAD HTNIRVRSLC
VQNVPRSGPP DDLLDMFGIS ARHIVEAVKK Y
//
