ID A0A0L6UYB8_9BASI Unreviewed; 640 AA.
AC A0A0L6UYB8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Transketolase-like pyrimidine-binding domain-containing protein {ECO:0000259|SMART:SM00861};
GN ORFNames=VP01_342g3 {ECO:0000313|EMBL:KNZ52840.1};
OS Puccinia sorghi.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=27349 {ECO:0000313|EMBL:KNZ52840.1, ECO:0000313|Proteomes:UP000037035};
RN [1] {ECO:0000313|EMBL:KNZ52840.1, ECO:0000313|Proteomes:UP000037035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RO10H11247 {ECO:0000313|EMBL:KNZ52840.1,
RC ECO:0000313|Proteomes:UP000037035};
RA Rochi L., Burguener G., Darino M., Turjanski A., Kreff E., Dieguez M.J.,
RA Sacco F.;
RT "Next Generation Sequencing and Analysis of the Genome of Puccinia sorghi L
RT Schw, the Causal Agent of Maize Common Rust.";
RL Submitted (AUG-2015) 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=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:KNZ52840.1}.
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; LAVV01008424; KNZ52840.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L6UYB8; -.
DR STRING; 27349.A0A0L6UYB8; -.
DR VEuPathDB; FungiDB:VP01_342g3; -.
DR OrthoDB; 1691772at2759; -.
DR Proteomes; UP000037035; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006163; P:purine nucleotide metabolic process; IEA:UniProt.
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; IPR033248; Transketolase_C.
DR InterPro; IPR005474; Transketolase_N.
DR PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR PANTHER; PTHR43825:SF1; TRANSKETOLASE-LIKE PYRIMIDINE-BINDING DOMAIN-CONTAINING PROTEIN; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000037035}.
FT DOMAIN 324..493
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 640 AA; 69849 MW; 3EB499FACAE5C4B5 CRC64;
MSCDKFPIPF VEKFHKVVLD PAQPQLSADQ KSKLLENISI LRDAIVFFTA TGAARGVSGH
TGGPFDTVPE VCLLLALFAS DPDGKKFDHT FWDEAGHRVA TQYLVAALEG HLPAEQLMMY
REAQSKLPGH PELGLTPGVK FSSGRLGHMW PLVNGVAMAH RNKTVFCLGS DGSQQEGNDA
EAARLAVAQN LNIKLLIDDN DVTIAGHPSV YMKGYEVSKT LEGHGLKVFH AEGENIESLW
QGLCAVIQCE GPAALIAKRV MCPGIQGLEG SNHGHDVIPV DKAISYLKDR PYGDAAAKIL
KSLTPSASPY LYIGSTKEKD ACRVQFGKAV NMVLDKLSKE EAKDKVMVID SDLEGSTGLK
AIRESHPEVF VPSGIMERGN FSAAAGFGFE KGKVGIFSTF SAFLEMCCSE ITMARLNRCN
VLCHFSHSGV DEMCDNTCHF GLNTFFADNG LEDGYPTRLY FPADVHQMTA IVKKVFWDMG
LRFVFSTRSK VPNILKEGTQ DPYFGGDYEF MPGKDEFIRR GSLGTVICFG EIVHRALDAV
DRLREEGFDV GLVNKSTLNV VDEEAMAQYG KQKFVLVAES LNQKTGLGSK MGTWLLERGL
TPRYGYIGTN KEGCGGLSAQ IFHQGLDPAS IIRKVKVLAA
//
