ID A0A0D2CR18_9EURO Unreviewed; 684 AA.
AC A0A0D2CR18;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=PV07_00491 {ECO:0000313|EMBL:KIW33658.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW33658.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW33658.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW33658.1,
RC ECO:0000313|Proteomes:UP000054466};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL Submitted (JAN-2015) 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}.
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DR EMBL; KN847040; KIW33658.1; -; Genomic_DNA.
DR RefSeq; XP_016253874.1; XM_016386946.1.
DR AlphaFoldDB; A0A0D2CR18; -.
DR STRING; 569365.A0A0D2CR18; -.
DR GeneID; 27339685; -.
DR VEuPathDB; FungiDB:PV07_00491; -.
DR HOGENOM; CLU_009227_0_0_1; -.
DR OrthoDB; 5399939at2759; -.
DR Proteomes; UP000054466; 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:SF2; TRANSKETOLASE 1-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:UP000054466};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 356..532
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 684 AA; 74721 MW; E6C414971E2D35FE CRC64;
MGYSDLDWKA VNTIRLLAVD ATLKANSGHP GAPMGMAPVA HVLFNKFMTF NPKNPNYINR
DRFVLSNGHG CMLQYALLHL FGYAVSMDDL KHFRQVDSIT PGHPEAHDTP GIEVTTGPLG
QGFSNAVGLA IAQAHTGAVF NKPGYDLINN YTYCFFGDGC AMEGVASEAA SVAGHLQLGN
LICIYDDNHI SIDGDTKVAF TEDVVKRFEA YGWHVQHVKD GDHDLEGIEA AIKKAKEVKD
KPSMIKLTTT IGFGSKLQGT GGVHGNPLKA DDAAQVKQKF GFNPEESFVV PQEVYDLYHK
HASEGAAAEQ AWNDLFKKYG SEFPELAKDF SRRLSRKLPE GWEKTLPVWK PTDAAVATRK
TSEKVLECIH EAVPELLSGS ADLTGSNNTR WKNAVDFQPP SLGIGDWTGR YLRYGVREHA
MAAIMNGISA YGTLIPAGGT FLNFVSYAAG AVRLSSLSHQ RVIYVATHDS IGLGEDGPTH
QPIETLVHFR ALPNMMVWRP ADGNETSAAY YMALTSTSTP SILALTRQNL PQLENSTIEN
AIKGGYVAVE AQNADITLVS TGSEVGLCVD TIKVLKDQHG LTARVVSMPC TEVFDAQPKD
YQLKVIPDGI PALSVEVMST LGWEKYSHEQ FGLNRFGASG PYKEVYKKFE FTPEGIAKRA
VATVEFYKGL KPRSPINRAF QQLI
//
