ID E3NWD4_CAERE Unreviewed; 482 AA.
AC E3NWD4;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=CRE_26040 {ECO:0000313|EMBL:EFP01903.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) 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}.
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DR EMBL; DS271490; EFP01903.1; -; Genomic_DNA.
DR RefSeq; XP_003087287.1; XM_003087239.1.
DR AlphaFoldDB; E3NWD4; -.
DR STRING; 31234.E3NWD4; -.
DR EnsemblMetazoa; CRE26040.1; CRE26040.1; WBGene00074556.
DR eggNOG; KOG0523; Eukaryota.
DR HOGENOM; CLU_009227_3_0_1; -.
DR InParanoid; E3NWD4; -.
DR OMA; ADYMRGS; -.
DR OrthoDB; 178912at2759; -.
DR Proteomes; UP000008281; 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; IPR005474; Transketolase_N.
DR PANTHER; PTHR43195:SF1; FI06132P-RELATED; 1.
DR PANTHER; PTHR43195; TRANSKETOLASE; 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.
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:UP000008281};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 270..434
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 482 AA; 51840 MW; 8D1A1266CEB78D7C CRC64;
MSTLFFSEMK YDVAEPKSAS ADRFILSKGH ACPILYAAWE EAGLLSHEQV LSLRKIDSDI
EGHPTPRLNF IDVATGSLGQ GLGVATGMAY VGKYIDKASY RVFCLLGDGE SAEGSVWEAA
AFASIYKLDN LVAIVDVNRL GQSQATSLGH DVETYKARFA AFGFNAIIVD GHNVEELLAA
YETARNTKGK PTALIAKTLK GKGIEGIENE DNWHGKPVPA ETINAIKARF HGSQKGKLVA
QKPINDAPAI DLHVGSIKMP APEYKKGDKV ATRAAYGTAL AKLGDVNPRV IGLDGDTKNS
TFSEKLLKKH PDQFIECFIA EQNLVGVAVG AQCRDRTIPF TSTFAAFFTR ATDQIRMAAV
SFANLKCVGS HVGVSIGEDG PSQMALEDLA IFRTIPGATV FYPTDAVSAE RATELAANTK
GVVFIRTGRP ALPVLYDNEE PFHIGQAKVV KQSAEDKIVL VGSGVTLYES LKAAEELEKE
GW
//
