ID A0A183E4J5_9BILA Unreviewed; 417 AA.
AC A0A183E4J5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=GPUH_LOCUS15886 {ECO:0000313|EMBL:VDN26870.1};
OS Gongylonema pulchrum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Spiruroidea; Gongylonematidae; Gongylonema.
OX NCBI_TaxID=637853 {ECO:0000313|Proteomes:UP000050760, ECO:0000313|WBParaSite:GPUH_0001590801-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:GPUH_0001590801-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN26870.1, ECO:0000313|Proteomes:UP000271098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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=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 ---------------------------------------------------------------------------
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 EMBL; UYRT01083039; VDN26870.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A183E4J5; -.
DR WBParaSite; GPUH_0001590801-mRNA-1; GPUH_0001590801-mRNA-1; GPUH_0001590801.
DR Proteomes; UP000050760; Unplaced.
DR Proteomes; UP000271098; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR CDD; cd02012; TPP_TK; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR049557; Transketolase_CS.
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 SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000271098};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 14..272
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 313..389
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|Pfam:PF02779"
SQ SEQUENCE 417 AA; 45769 MW; C5B3A247CE2786AD CRC64;
MVGEKVEALE LYDMANRLRI SSIEMTAASK SGHPTSSCSA AEIVATLFFG EMKFDKKQPK
NPSADRFVLS KGHACPVLYA VWHELGHLTR DDMMSLRKLG SDIEGHPTPR LDFIDVATGS
LGQGLSCAAG MAYVGKYIDK ASYRVYCLLG DGECAEGSVW EAVGFASYYK LDNLVAIVDM
NRLGQTQQTM FGHDADALAK RFEAFGCHAI VVDGHNVEQL CDAYKSARET KHRPTAIVAK
TFKGKGIVGI EDENNWHGKP VPLDTIEPIR QLIVQKDDQL KLTNKTPIMD APDVHLPIGK
IKMAPPDYKV GEKVATRMAY GTALAKLGDV CSRIIGLDGD TKNSTFSEKL LGKHPDQFIE
CFIAEQNLVG VAVGLQCRDR AIPFARYFFF SAFDKVLRFL CKDPNLGLSA LSYIAST
//