ID A0A428SRA7_9HYPO Unreviewed; 727 AA.
AC A0A428SRA7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=CEP52_013883 {ECO:0000313|EMBL:RSL92307.1};
OS Fusarium oligoseptatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=2604345 {ECO:0000313|EMBL:RSL92307.1, ECO:0000313|Proteomes:UP000287144};
RN [1] {ECO:0000313|EMBL:RSL92307.1, ECO:0000313|Proteomes:UP000287144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL62579 {ECO:0000313|EMBL:RSL92307.1,
RC ECO:0000313|Proteomes:UP000287144};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737,
CC ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001027};
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:RSL92307.1}.
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DR EMBL; NKCK01000205; RSL92307.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428SRA7; -.
DR STRING; 1325735.A0A428SRA7; -.
DR Proteomes; UP000287144; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:UniProt.
DR GO; GO:0006163; P:purine nucleotide metabolic process; IEA:UniProt.
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; IPR005478; Transketolase_bac-like.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR049557; Transketolase_CS.
DR InterPro; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR NCBIfam; TIGR00232; tktlase_bact; 1.
DR PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR PANTHER; PTHR43522:SF6; TRANSKETOLASE-LIKE PYRIMIDINE-BINDING DOMAIN-CONTAINING PROTEIN-RELATED; 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; PS00801; TRANSKETOLASE_1; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000287144};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 384..567
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 727 AA; 80682 MW; DFB43F9ED6F36F0F CRC64;
MAPSAITPEP KEETVVGPNV LKLIQNEDAQ TIDVFLRQFR CLIADLCQQF NGGHPGGAMG
MAAIGLALWK YVMKYSPSNP DYFNRDRFVL SNGHTCLFQY TFLHLTGYKQ MTFDQLKSYH
SARYDSFAPG HPEIEHEGIE VTTGPLGQGI ANAVGLAMAT KHLAATYNKP GHELINNTTF
CMIGDACLQE GVALEAIQLA GHWKLNNLVV MYDNNQITCD GSVDLCNTED VNAKMRACGW
DVIEIEDGCY DVEGIVKALL KAKSSTDKPT FINVHTVIGV GSKVAGDAKA HGAAFSPDGV
KAVKEHFGMN PEEHFVVTDE IYNYFRDVKT RGERLEEDWK ALVASYAKEY PELHEEFIKR
VEGRFTEDWR SIIPAKESFP TTPTASRKSA GIICNPLAAK LKNFMVGTAD LSPSVNMIWK
DKVDFQHPDL KTTCGITGNY GGRYIHWGIR EHAMASISNG LAAYGKGTIL PITSSFFMFY
IYAAPGVRMG ALQNLQAIHI ATHDSIGTGE DGPTHQPIAL PNLYRSMPNL LYIRPCDTEE
TAGAFISALE AKDTPSIISL SRQNLEQYPQ YSSRDGAQKG AYVFIEEEDA DVTLIGVGAE
MCFAVKTRDV LKEKFNIKAR VVSFPCQRIF NKQSIEYKRD VLRYRTNAPR VVIEAYAVNG
WERYADAGFS MATFGKSLPG KDAYKFFGFD ENVIAPEVAK LVEEVKKEGI ESLRGEFRDL
NPVKHEH
//
